@article{MTMT:32695039,
	title = {Polyhydroxylated Cyclopentane β-Amino Acids Derived from d -Mannose and d -Galactose: Synthesis and Protocol for Incorporation into Peptides},
	url = {https://m2.mtmt.hu/api/publication/32695039},
	author = {Fernández, F. and Fernández, A.G. and Balo, R. and Sánchez-Pedregal, V.M. and Royo, M. and Soengas, R.G. and Estévez, R.J. and Estévez, J.C.},
	doi = {10.1021/acsomega.1c05468},
	journal-iso = {ACS OMEGA},
	journal = {ACS OMEGA},
	volume = {7},
	unique-id = {32695039},
	issn = {2470-1343},
	abstract = {A stereoselective synthesis of polyhydroxylated cyclopentane β-amino acids from hexoses is reported. The reaction sequence comprises, as key steps, ring-closing metathesis of a polysubstituted diene intermediate followed by the stereoselective aza-Michael functionalization of the resulting cyclopent-1-ene-1-carboxylic acid ester. Examples of synthesis of polysubstituted 2-aminocyclopentanecarboxylic acid derivatives starting from protected d-mannose and d-galactose are presented. A general protocol for the incorporation of these highly functionalized alicyclic β-amino acids into peptides is also reported. © 2022 The Authors. Published by American Chemical Society.},
	year = {2022},
	eissn = {2470-1343},
	pages = {2002-2014}
}

@article{MTMT:33167056,
	title = {Peptidomimetics and Their Applications for Opioid Peptide Drug Discovery},
	url = {https://m2.mtmt.hu/api/publication/33167056},
	author = {Lee, Yeon Sun},
	doi = {10.3390/biom12091241},
	journal-iso = {BIOMOLECULES},
	journal = {BIOMOLECULES},
	volume = {12},
	unique-id = {33167056},
	issn = {2218-273X},
	abstract = {Despite various advantages, opioid peptides have been limited in their therapeutic uses due to the main drawbacks in metabolic stability, blood-brain barrier permeability, and bioavailability. Therefore, extensive studies have focused on overcoming the problems and optimizing the therapeutic potential. Currently, numerous peptide-based drugs are being marketed thanks to new synthetic strategies for optimizing metabolism and alternative routes of administration. This tutorial review briefly introduces the history and role of natural opioid peptides and highlights the key findings on their structure-activity relationships for the opioid receptors. It discusses details on opioid peptidomimetics applied to develop therapeutic candidates for the treatment of pain from the pharmacological and structural points of view. The main focus is the current status of various mimetic tools and the successful applications summarized in tables and figures.},
	keywords = {BIOAVAILABILITY; peptidomimetic; ANALGESIC DRUGS; opioid receptors; peptide backbone modifications; locally constrained peptides},
	year = {2022},
	eissn = {2218-273X},
	orcid-numbers = {Lee, Yeon Sun/0000-0002-0472-4765}
}

@article{MTMT:32619226,
	title = {Synthesis, pharmacological evaluation, and computational studies of cyclic opioid peptidomimetics containing β3-lysine},
	url = {https://m2.mtmt.hu/api/publication/32619226},
	author = {Wtorek, K. and Lipiński, P.F.J. and Adamska-Bartłomiejczyk, A. and Piekielna-Ciesielska, J. and Sukiennik, J. and Kluczyk, A. and Janecka, A.},
	doi = {10.3390/molecules27010151},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {27},
	unique-id = {32619226},
	issn = {1420-3049},
	abstract = {Our formerly described pentapeptide opioid analog Tyr-c[D-Lys-Phe-Phe-Asp]NH2 (desig-nated RP-170), showing high affinity for the mu (MOR) and kappa (KOR) opioid receptors, was much more stable than endomorphine-2 (EM-2) in the rat brain homogenate and displayed remarkable antinociceptive activity after central (intracerebroventricular) and peripheral (intravenous) admin-istration. In this report, we describe the further modification of this analog, which includes the incorporation of a β3-amino acid, (R)-and (S)-β3-Lys, instead of D-Lys in position 2. The influence of such replacement on the biological properties of the obtained analogs, Tyr-c[(R)-β3-Lys-Phe-Phe-Asp]NH2 (RP-171) and Tyr-c[(S)-β3-Lys-Phe-Phe-Asp]NH2, (RP-172), was investigated in vitro. Receptor radiolabeled displacement and functional calcium mobilization assays were performed to measure binding affinity and receptor activation of the new analogs. The obtained data revealed that only one of the diastereoisomeric peptides, RP-171, was able to selectively bind and activate MOR. Molecular modeling (docking and molecular dynamics (MD) simulations) suggests that both compounds should be accommodated in the MOR binding site. However, in the case of the inactive isomer RP-172, fewer hydrogen bonds, as well as instability of the canonical ionic interaction to Asp147, could explain its very low MOR affinity. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.},
	keywords = {PEPTIDE SYNTHESIS; opioid receptors; β-amino acids; functional assay; Receptor binding studies},
	year = {2022},
	eissn = {1420-3049}
}

@article{MTMT:32334776,
	title = {Selective MOR activity of DAPEA and Endomorphin-2 analogues containing a (R)-γ-Freidinger lactam in position two},
	url = {https://m2.mtmt.hu/api/publication/32334776},
	author = {Della, Valle A. and Stefanucci, A. and Scioli, G. and Szűcs, Edina and Benyhe, Sándor and Pieretti, S. and Minosi, P. and Sturaro, C. and Calò, G. and Zengin, G. and Mollica, A.},
	doi = {10.1016/j.bioorg.2021.105219},
	journal-iso = {BIOORG CHEM},
	journal = {BIOORGANIC CHEMISTRY},
	volume = {115},
	unique-id = {32334776},
	issn = {0045-2068},
	abstract = {The use of α-amino-γ lactam of Freidinger (Agl) may serve as an impressive method to increase the biological stability of peptides and an appropriate tool to elucidate their structure-activity relationships. The endomorphin-2 (EM-2) and [D-Ala2, des-Leu5] enkephalin amide (DAPEA) are two linear opioid tetrapeptides agonists of MOR and MOR/DOR respectively. Herein, we investigated the influence of the incorporation of (R/S)-Agl in position 2 and 3 on the biological profile of the aforementioned products in vitro and in vivo. Receptor radiolabeled displacement and functional assays were used to measure in vitro the binding affinity and receptors activation of the novel analogues. The mouse tail flick and formalin tests allowed to observe their antinociceptive effect in vivo. Data revealed that peptide A2D was able to selectively bind and activate MOR with a potent antinociceptive effect after intracerebroventricular (i.c.v.) administration, performing better than the parent compounds EM-2 and DAPEA. Molecular docking calculations helped us to understand the key role exerted by the Freidinger Agl moiety in A2D for the interaction with the MOR binding pocket. © 2021 Elsevier Inc.},
	year = {2021},
	eissn = {1090-2120}
}

@article{MTMT:31432758,
	title = {beta(2)-Homo-Amino Acid Scan of mu-Selective Opioid Tetrapeptide TAPP},
	url = {https://m2.mtmt.hu/api/publication/31432758},
	author = {Tymecka, Dagmara and Lipinski, Piotr F. J. and Kosson, Piotr and Misicka, Aleksandra},
	doi = {10.3390/molecules25102461},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {25},
	unique-id = {31432758},
	issn = {1420-3049},
	abstract = {TAPP (H-Tyr-d-Ala-Phe-Phe-NH2) is a potent, mu -selective opioid ligand. In order to gain further insights into pharmacophoric features of this tetrapeptide, we have performed a beta (2)-Homo-amino acid (beta (2)hAA) scan of the TAPP sequence. To this aim, 10 novel analogues have been synthesized and evaluated for mu -opioid and delta -opioid receptor affinity as well as for stability in human plasma. The derivatives included compounds in which a (R)- or (S)-beta (2)-Homo-Homologue replaced the amino acids in the TAPP sequence. The derivatives with (R)- or (S)-beta (2)hPhe(4) turned out to bind mu OR with affinities equal to that of the parent. beta (2)hAAs in position 1 and 3 resulted in rather large affinity decreases, but the change differed depending on the stereochemistry. beta (2)-Homologation in the second position gave derivatives with very poor mu OR binding. According to molecular modelling, the presented alpha/beta -peptides adopt a variety of binding poses with their common element being an ionic interaction between a protonable amine of the first residue and Asp147. A feature required for high mu OR affinity seems the ability to accommodate the ring in the fourth residue in a manner similar to that found for TAPP. Contrary to what might be expected, several compounds were significantly less stable in human plasma than the parent compound.},
	keywords = {MU-OPIOID RECEPTOR; opioid peptides; TAPP; beta(2)-amino acids; beta(2)-Homo-amino acids; racemic synthesis of beta(2)-amino acids},
	year = {2020},
	eissn = {1420-3049},
	orcid-numbers = {Misicka, Aleksandra/0000-0001-7446-2396}
}

@article{MTMT:31335726,
	title = {The search for opioid analgesics with limited tolerance liability},
	url = {https://m2.mtmt.hu/api/publication/31335726},
	author = {Wtorek, Karol and Piekielna-Ciesielska, Justyna and Janecki, Tomasz and Janecka, Anna},
	doi = {10.1016/j.peptides.2020.170331},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {130},
	unique-id = {31335726},
	issn = {0196-9781},
	year = {2020},
	eissn = {1873-5169},
	orcid-numbers = {Janecka, Anna/0000-0001-5178-4464}
}

@article{MTMT:31423916,
	title = {Design, synthesis, and biological activity of new endomorphin analogs with multi-site modifications},
	url = {https://m2.mtmt.hu/api/publication/31423916},
	author = {Zhao, Long and Luo, Keyao and Wang, Zhaojuan and Wang, Yuan and Zhang, Xianghui and Yang, Dongxu and Ma, Mengtao and Zhou, Jingjing and Cui, Jiaming and Wang, Jing and Han, Chao-Zhen-yi and Liu, Xin and Wang, Rui},
	doi = {10.1016/j.bmc.2020.115438},
	journal-iso = {BIOORGAN MED CHEM},
	journal = {BIOORGANIC & MEDICINAL CHEMISTRY},
	volume = {28},
	unique-id = {31423916},
	issn = {0968-0896},
	abstract = {Endomorphin (EM)-1 and EM-2 are the most effective endogenous analgesics with efficient separation of analgesia from the risk of adverse effects. Poor metabolic stability and ineffective analgesia after peripheral administration were detrimental for the use of EMs as novel clinical analgesics. Therefore, here, we aimed to establish new EM analogs via introducing different bifunctional D-amino acids at position 2 of [(2-furyl)Map(4)] EMs. The combination of [(2-furyl)Map4]EMs with D-Arg(2) or D-Cit(2) yielded analogs with enhanced binding affinity to the mu-opioid receptor (MOR) and increased stability against enzymatic degradation (t(1/2) > 300 min). However, the agonistic activities of these analogs toward MOR were slightly reduced. Similar to morphine, peripheral administration of the analog [D-Cit(2), (2-furyl)Map(4)]EM-1 (10) significantly inhibited the pain behavior of mice in multiple pain models. In addition, this EM-1 analog was associated with reduced tolerance, less effect on gastrointestinal mobility, and no significant motor impairment. Compared to natural EMs, the EM analogs synthesized herein had enhanced metabolic stability, bioavailability, and analgesic properties.},
	keywords = {ANALGESIA; MU-OPIOID RECEPTOR; Motor impairment; Adverse effect; Endomorphin},
	year = {2020},
	eissn = {1464-3391}
}

@article{MTMT:30901973,
	title = {Endomorphin-2 analogs containing modified tyrosines: Biological and theoretical investigation of the influence on conformation and pharmacological profile},
	url = {https://m2.mtmt.hu/api/publication/30901973},
	author = {Wtorek, Karol and Artali, Roberto and Piekielna-Ciesielska, Justyna and Koszuk, Jacek and Kluczyk, Alicja and Gentilucci, Luca and Janecka, Anna},
	doi = {10.1016/j.ejmech.2019.06.077},
	journal-iso = {EUR J MED CHEM},
	journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {179},
	unique-id = {30901973},
	issn = {0223-5234},
	abstract = {New analogs of the endogenous opioid agonist endomorphin-2 (EM-2, H-Tyr-Pro-Phe-Phe-NH2) have been obtained by introducing modified tyrosines at the position 1 of the sequence. For all analogs, the cis/trans conformation ratio about the tyramine-Pro amide bond, lipophilicity, receptor affinities, and functional activities, have been determined. Among the novel derivatives, [Dmt(3'-Cl)](EM)-E-1-2 (4) stood out for its subnanomolar mu-opioid receptor affinity and potent agonist activity, superior to that of the parent peptide EM-2. Hybrid quantum mechanics/molecular mechanics docking computations supported the cis tyramine-Pro bioactive conformation, and allowed us to analyze the contribution of the substituents of the "message" tyramine to binding, highlighting the role of halogen-bonding in the higher receptor affinity of peptide 4. (C) 2019 Elsevier Masson SAS. All rights reserved.},
	keywords = {opioid peptides; Molecular docking; Tyrosine analogs; Halogen-bond},
	year = {2019},
	eissn = {1768-3254},
	pages = {527-536},
	orcid-numbers = {Wtorek, Karol/0000-0002-3567-6962; Janecka, Anna/0000-0001-5178-4464}
}

@article{MTMT:27602829,
	title = {Constraining Endomorphin-1 by beta,alpha-Hybrid Dipeptide/Heterocycle Scaffolds: Identification of a Novel k-Opioid Receptor Selective Partial Agonist},
	url = {https://m2.mtmt.hu/api/publication/27602829},
	author = {De Marco, Rossella and Bedini, Andrea and Spampinato, Santi and Comellini, Lorenzo and Zhao, Junwei and Artali, Roberto and Gentilucci, Luca},
	doi = {10.1021/acs.jmedchem.8b00296},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {61},
	unique-id = {27602829},
	issn = {0022-2623},
	year = {2018},
	eissn = {1520-4804},
	pages = {5751-5757}
}

@article{MTMT:26919611,
	title = {Using β-amino acids and β-peptide templates to create bioactive ligands and biomaterials},
	url = {https://m2.mtmt.hu/api/publication/26919611},
	author = {Del Borgo, Mark P and Kulkarni, Ketav and Aguilar, Marie-Isabel},
	doi = {10.2174/1381612823666170616083031},
	journal-iso = {CURR PHARM DESIGN},
	journal = {CURRENT PHARMACEUTICAL DESIGN},
	volume = {23},
	unique-id = {26919611},
	issn = {1381-6128},
	abstract = {β-Amino acids are being increasingly used in the design of bioactive ligands and more recently in the generation of novel biomaterials. Peptides containing either individual β-amino acid substitutions or peptides comprised entirely of β-amino acids, display unique properties in terms of their structural and/or chemical characteristics. β Peptides form well-defined secondary structures that exhibit different geometries compared to the corresponding α-peptides. β-Peptides, including α-peptides containing only one or two β-amino acids, can be easily modified with different functional groups and are metabolically stable and, together with the predictable side chain topography, have led to the design of a growing number of bioactive β-peptides with a range of biological targets and therapeutic applications. More recently, our understanding of the folding and self-assembly of β-peptides has resulted in the generation of novel biomaterials. The focus of this review is to examine how the structural and chemical properties of β-peptides have been exploited in the design of bioactive peptides and selfassembled nanomaterials. © 2017 Bentham Science Publishers.},
	keywords = {Animals; Humans; PEPTIDES; PEPTIDE; GENETICS; LIGAND; ARTICLE; LIGANDS; PROTEIN SECONDARY STRUCTURE; human; animal; Tissue regeneration; Chemistry; amino acid sequence; amino acid substitution; priority journal; nonhuman; Protein Structure, Tertiary; enzyme inhibition; Templates, Genetic; Protein Folding; DRUG DESIGN; cardiovascular diseases; cardiovascular disease; unclassified drug; Neoplasms; physical chemistry; drug structure; biomaterial; TRENDS; amino acid; amino acids; self-assembly; peptidomimetic; supramolecular chemistry; neoplasm; enzyme inhibitor; protein protein interaction; Protein Structure, Secondary; ANTIMICROBIAL ACTIVITY; Biocompatible Materials; DRUG DISCOVERY; beta amino acid; protein structure; cell function; drug development; nanomaterial; Biomaterials; DNA template; protein tertiary structure; polypeptide antibiotic agent; protein assembly; Protein Engineering; β-amino acids; beta peptide; β-Peptides; procedures; IC50; alpha peptide; proteolytic stability; Bioactive ligand},
	year = {2017},
	eissn = {1873-4286},
	pages = {3772-3785}
}

@article{MTMT:27071456,
	title = {Tryptophan-Containing Non-Cationizable Opioid Peptides - a new chemotype with unusual structure and in vivo activity},
	url = {https://m2.mtmt.hu/api/publication/27071456},
	author = {De Marco, Rossella and Gentilucci, Luca},
	doi = {10.4155/fmc-2017-0104},
	journal-iso = {FUTURE MED CHEM},
	journal = {FUTURE MEDICINAL CHEMISTRY},
	volume = {9},
	unique-id = {27071456},
	issn = {1756-8919},
	year = {2017},
	eissn = {1756-8927},
	pages = {2099-2115}
}

@article{MTMT:26898077,
	title = {Synthesis and activity of opioid peptidomimetics with beta(2)- and beta(3)-amino acids},
	url = {https://m2.mtmt.hu/api/publication/26898077},
	author = {Gach-Janczak, Katarzyna and Piekielna-Ciesielska, Justyna and Adamska-Bartlomiejczyk, Anna and Perlikowska, Renata and Kruszynski, Rafal and Kluczyk, Alicja and Krzywik, Julia and Sukiennik, Jaroslaw and Cerlesi, Maria Camilla and Calo, Girolamo and Wasilewski, Andrzej and Zielinska, Marta and Janecka, Anna},
	doi = {10.1016/j.peptides.2017.07.015},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {95},
	unique-id = {26898077},
	issn = {0196-9781},
	year = {2017},
	eissn = {1873-5169},
	pages = {116-123}
}

@article{MTMT:3029039,
	title = {Synthesis, biological evaluation and structural analysis of novel peripherally active morphiceptin analogs},
	url = {https://m2.mtmt.hu/api/publication/3029039},
	author = {Adamska, A and Kluczyk, A and Cerlesi, MC and Calo, G and Janecka, A and Borics, Attila},
	doi = {10.1016/j.bmc.2016.02.034},
	journal-iso = {BIOORGAN MED CHEM},
	journal = {BIOORGANIC & MEDICINAL CHEMISTRY},
	volume = {24},
	unique-id = {3029039},
	issn = {0968-0896},
	year = {2016},
	eissn = {1464-3391},
	pages = {1582-1588}
}

@article{MTMT:25383078,
	title = {Biphalin analogs containing beta(3)-homo-amino acids at the 4,4 ' positions: Synthesis and opioid activity profiles},
	url = {https://m2.mtmt.hu/api/publication/25383078},
	author = {Fraczak, Oliwia and Lasota, Anika and Kosson, Piotr and Lesniak, Anna and Muchowska, Adriana and Lipkowski, Andrzej W and Olma, Aleksandra},
	doi = {10.1016/j.peptides.2015.02.004},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {66},
	unique-id = {25383078},
	issn = {0196-9781},
	year = {2015},
	eissn = {1873-5169},
	pages = {13-18}
}

@article{MTMT:25791119,
	title = {Synthesis and biological evaluations of novel endomorphin analogues containing alpha-hydroxy-beta-phenylalanine (AHPBA) displaying mixed mu/delta opioid receptor agonist and delta opioid receptor antagonist activities},
	url = {https://m2.mtmt.hu/api/publication/25791119},
	author = {Hu, Miao and Giulianotti, Marc A and McLaughlin, Jay P and Shao, Jiaan and Debevec, Ginamarie and Maida, Laura E and Geer, Phaedra and Cazares, Margaret and Misler, Jaime and Li, Ling and Dooley, Colette and Ganno, Michelle L and Eans, Shainnel O and Mizrachi, Elisa and Santos, Radleigh G and Yongye, Austin B and Houghten, Richard A and Yu, Yongping},
	doi = {10.1016/j.ejmech.2014.12.049},
	journal-iso = {EUR J MED CHEM},
	journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {92},
	unique-id = {25791119},
	issn = {0223-5234},
	year = {2015},
	eissn = {1768-3254},
	pages = {270-281}
}

@{MTMT:30332200,
	title = {Rational approach to the design of bioactive peptidomimetics: Recent developments in opioid agonist peptides},
	url = {https://m2.mtmt.hu/api/publication/30332200},
	author = {Mollica, A. and Stefanucci, A. and Costante, R. and Hruby, V.J.},
	booktitle = {Studies in Natural Products Chemistry},
	doi = {10.1016/B978-0-444-63462-7.00002-6},
	volume = {46},
	unique-id = {30332200},
	abstract = {Pharmacological management of severe and chronic pain remains a difficult achievement with currently available analgesic drugs. The design and development of potent opioid analogs with reduced tolerance, dependence, respiratory depression, and other unwanted side effects, could be of great value in the clinical treatment of chronic pain. The hierarchical approach to peptidomimetic design has dramatically advanced over the past three decades; a significant target in research since the discovery of multiple opioid receptors has been to develop highly potent and selective opioid receptor peptidomimetics that overcome the problems related to scarce bioavailability, enzymatic degradation, and low safety profile of natural peptides. Peptide drug design is a high multidisciplinary area that often relies on the state-of-the-art of organic chemistry, pharmacology, and biochemistry, computational methods and biophysical methods for determining the structural, conformational, topographical, and dynamic properties of designed ligands. With the aim to explore the recent advancements in opioids research, in this chapter, particular attention has been paid on the structural modifications of natural opioid peptides to obtain potent, selective, and stable opioid agonists. In addition, we focused our attention on μ/δ mixed agonists and novel approaches based on multitarget ligands, as discussed in section "Future Perspectives and Conclusions." © 2015 Elsevier B.V.},
	keywords = {opioid receptor agonists antinociceptive profile peptidomimetics topographical constraints structure-activity relationship},
	year = {2015},
	pages = {27-68}
}

@article{MTMT:2817673,
	title = {Peptides containing β-amino acid patterns: Challenges and successes in medicinal chemistry},
	url = {https://m2.mtmt.hu/api/publication/2817673},
	author = {Cabrele, C and Martinek, Tamás and Reiser, O and Berlicki, Ł},
	doi = {10.1021/jm5010896},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {57},
	unique-id = {2817673},
	issn = {0022-2623},
	abstract = {The construction of bioactive peptides using β-amino acid-containing sequence patterns is a very promising strategy to obtain analogues that exhibit properties of high interest for medicinal chemistry applications. β-Amino acids have been shown to modulate the conformation, dynamics, and proteolytic susceptibility of native peptides. They can be either combined with α-amino acids by following specific patterns, which results in backbone architectures with well-defined orientations of the side chain functional groups, or assembled in de novo-designed bioactive β- or α,β-peptidic sequences. Such peptides display various biological functions, including antimicrobial activity, inhibition of protein-protein interactions, agonism/antagonism of GPCR ligands, and anti-angiogenic activity.},
	year = {2014},
	eissn = {1520-4804},
	pages = {9718-9739},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:2547618,
	title = {Enantioseparation of β2-amino acids on cinchona alkaloid-based zwitterionic chiral stationary phases. Structural and temperature effects},
	url = {https://m2.mtmt.hu/api/publication/2547618},
	author = {Ilisz, István and Grecsó, Nóra and Aranyi, Anita and Suchotin, P and Tymecka, D and Wilenska, B and Misicka, A and Fülöp, Ferenc and Lindner, W and Péter, Antal},
	doi = {10.1016/j.chroma.2014.01.075},
	journal-iso = {J CHROMATOGR A},
	journal = {JOURNAL OF CHROMATOGRAPHY A},
	volume = {1334},
	unique-id = {2547618},
	issn = {0021-9673},
	abstract = {The enantiomers of sixteen unusual β2-amino acids were directly separated on chiral stationary phases containing quinine- or quinidine-based zwitterionic selectors. The effects of the mobile phase composition, the structure of the analyte and temperature on the separations were investigated. Experiments were performed at constant mobile phase compositions in the temperature range -5 to 55°C in order to study the effects of temperature, and thermodynamic parameters were estimated from plots of lnk or lnα vs. 1/T. Some mechanistic aspects of the chiral recognition process are discussed with respect to the structures of the analytes. It was found that the enantiomeric separations were in most cases enthalpically driven, but entropically driven separation was also observed. The sequence of elution of the enantiomers was determined in some cases. © 2014 Elsevier B.V.},
	keywords = {liquid chromatography; Temperature dependence of enantioseparation; Quinine- and quinidine-based chiral zwitterionic ion-exchanger selectors; β2-Amino acids},
	year = {2014},
	eissn = {1873-3778},
	pages = {44-54},
	orcid-numbers = {Ilisz, István/0000-0001-8282-457X; Grecsó, Nóra/0000-0003-4323-1872; Fülöp, Ferenc/0000-0003-1066-5287}
}

@mastersthesis{MTMT:30615868,
	title = {SYNTHESIS, STRUCTURAL INVESTIGATION AND BIOLOGICAL EVALUATION OF CONFORMATIONALLY CONSTRAINED PEPTIDOMIMETICS},
	url = {https://m2.mtmt.hu/api/publication/30615868},
	author = {Airaghi, Francesco},
	publisher = {University of Milano},
	unique-id = {30615868},
	abstract = {This Ph.D. thesis is located in the medicinal chemistry research field. Peptides are among the most studied entities as potential drug candidates, due to their natural abundance and biological implications. However, as drugs they possess several disadvantages because of low bioavailability and short half-life. Peptidomimetics try to overcome such drawbacks, maintaining meanwhile the biological activity. These mimics can also be useful to define bioactive forms of natural peptides, for instance through insertion of conformational constrictions able to reduce the peptide inherent flexibility. Thus, I explored the synthesis and the evaluation of some conformationally constrained peptidomimetics which potentially could be employed into different scientific fields and pharmaceutical contexts. Once prepared these scaffolds, I evaluated their secondary structure by means of spectroscopic methods including NMR and IR techniques. After insertion into more complex structures, strictly related to biologically active compounds, I verified their therapeutic potential. In some cases I could achieve very interesting biological results, in the range of activity of the natural corresponding peptides or of the reference lead compounds. I also tried to rationalize the biological activity outcomes, by joining them with molecular mechanics and docking-based structural investigation.},
	year = {2013}
}

@article{MTMT:23594314,
	title = {Structural and Biological Exploration of Phe(3)-Phe(4)-Modified Endomorphin-2 Peptidomimetics},
	url = {https://m2.mtmt.hu/api/publication/23594314},
	author = {Lesma, G and Salvadori, S and Airaghi, F and Murray, TF and Recca, T and Sacchetti, A and Balboni, G and Silvani, A},
	doi = {10.1021/ml400189r},
	journal-iso = {ACS MED CHEM LETT},
	journal = {ACS MEDICINAL CHEMISTRY LETTERS},
	volume = {4},
	unique-id = {23594314},
	issn = {1948-5875},
	year = {2013},
	pages = {795-799}
}

@article{MTMT:2208938,
	title = {Synthesis, pharmacological evaluation and conformational investigation of endomorphin-2 hybrid analogues},
	url = {https://m2.mtmt.hu/api/publication/2208938},
	author = {Lesma, G and Salvadori, S and Airaghi, F and Bojnik, Engin and Borsodi, Anna and Recca, T and Sacchetti, A and Balboni, G and Silvani, A},
	doi = {10.1007/s11030-012-9399-5},
	journal-iso = {MOL DIVERS},
	journal = {MOLECULAR DIVERSITY},
	volume = {17},
	unique-id = {2208938},
	issn = {1381-1991},
	abstract = {This study reports on new pharmacologically active endomorphin-2 analogues, incorporating β 2-hPhe, β 3-hPhe and β 3-hTic unnatural amino acids in the place of the Phe 3-Phe 4residues. Such α, β-hybrid analogues were designed to exploit the great potential of β-amino acids in generating conformational variation at the key positions 3 and 4, with the aim of evaluating the effect on the opioid binding affinity. Ligand-stimulated binding assays indicated that some analogues retained a significant affinity, especially for the δ receptor. 1H NMR and molecular modelling suggested the predominance of bent structures for all compounds. The molecular docking with the μ-opioid receptor model was also performed, highlighting a common binding mode for active compounds and helping to rationalize the observed structure-activity data. © 2012 Springer Science+Business Media Dordrecht.},
	keywords = {OPIOID RECEPTOR; ENDOMORPHIN-2; beta-amino acid; molecular modelling; peptidomimetic; Molecular docking},
	year = {2013},
	eissn = {1573-501X},
	pages = {19-31}
}

@article{MTMT:24536999,
	title = {Design, Synthesis, and Pharmacological Characterization of Novel Endomorphin-1 Analogues as Extremely Potent mu-Opioid Agonists},
	url = {https://m2.mtmt.hu/api/publication/24536999},
	author = {Liu, X and Wang, Y and Xing, YH and Yu, J and Ji, H and Kai, M and Wang, ZL and Wang, D and Zhang, YX and Zhao, DP and Wang, R},
	doi = {10.1021/jm400195y},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {56},
	unique-id = {24536999},
	issn = {0022-2623},
	year = {2013},
	eissn = {1520-4804},
	pages = {3102-3114}
}

@article{MTMT:2486869,
	title = {Ligand-Specific Regulation of the Endogenous Mu-Opioid Receptor by Chronic Treatment with Mu-Opioid Peptide Agonists},
	url = {https://m2.mtmt.hu/api/publication/2486869},
	author = {Muranyi, M and Cinar, Resat and Kékesi, Orsolya Sára and Birkás, Erika and Fábián, Gabriella and Bozó, Bea and Zentai, A and Tóth, Géza and Kicsi, EG and Macsai, M and Dochnal, Roberta and Szabó, Gyula and Szűcs, Mária},
	doi = {10.1155/2013/501086},
	journal-iso = {BIOMED RES INT},
	journal = {BIOMED RESEARCH INTERNATIONAL},
	volume = {2013},
	unique-id = {2486869},
	issn = {2314-6133},
	abstract = {Since the discovery of the endomorphins (EM), the postulated endogenous peptide agonists of the mu-opioid receptors, several analogues have been synthesized to improve their binding and pharmacological profiles. We have shown previously that a new analogue, cis-1S,2R-aminocyclohexanecarboxylic acid(2)-endomorphin-2 (ACHC-EM2), had elevated mu-receptor affinity, selectivity, and proteolytic stability over the parent compound. In the present work, we have studied its antinociceptive effects and receptor regulatory processes. ACHC-EM2 displayed a somewhat higher (60%) acute antinociceptive response than the parent peptide, EM2 (45%), which peaked at 10 min after intracerebroventricular (icv) administration in the rat tail-flick test. Analgesic tolerance developed to the antinociceptive effect of ACHC-EM2 upon its repeated icv injection that was complete by a 10-day treatment. This was accompanied by attenuated coupling of mu-sites to G-proteins in subcellular fractions of rat brain. Also, the density of mu-receptors was upregulated by about 40% in the light membrane fraction, with no detectable changes in surface binding. Distinct receptor regulatory processes were noted in subcellular fractions of rat brains made tolerant by the prototypic full mu-agonist peptide, DAMGO, and its chloromethyl ketone derivative, DAMCK. These results are discussed in light of the recently discovered phenomenon, that is, the "so-called biased agonism" or "functional selectivity".},
	keywords = {IN-VIVO; RAT-BRAIN; DESENSITIZATION; TOLERANCE; MORPHINE; internalization; BIASED AGONISM; FUNCTIONAL SELECTIVITY; BETA-ARRESTIN; G-protein activation},
	year = {2013},
	eissn = {2314-6141},
	orcid-numbers = {Fábián, Gabriella/0000-0002-2323-4948; Szabó, Gyula/0000-0002-3409-5357}
}

@article{MTMT:2489391,
	title = {Syntheses of four enantiomers of 2,3-diendo- and 3-endo-aminobicyclo[2.2.2] oct-5-ene-2-exo-carboxylic acid and their saturated analogues},
	url = {https://m2.mtmt.hu/api/publication/2489391},
	author = {Palkó, Márta and Hanninen, MM and Sillanpaa, R and Fülöp, Ferenc},
	doi = {10.3390/molecules181215080},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {18},
	unique-id = {2489391},
	issn = {1420-3049},
	year = {2013},
	eissn = {1420-3049},
	pages = {15080-15093},
	orcid-numbers = {Palkó, Márta/0000-0002-8265-7377; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:2877333,
	title = {Endomorphin Derivatives with Improved Pharmacological Properties},
	url = {https://m2.mtmt.hu/api/publication/2877333},
	author = {Varamini, P and Blanchfield, JT and Tóth, István},
	doi = {10.2174/0929867311320220002},
	journal-iso = {CURR MED CHEM},
	journal = {CURRENT MEDICINAL CHEMISTRY},
	volume = {20},
	unique-id = {2877333},
	issn = {0929-8673},
	year = {2013},
	eissn = {1875-533X},
	pages = {2741-2758}
}

@article{MTMT:2085025,
	title = {The Effect of Pro(2) Modifications on the Structural and Pharmacological Properties of Endomorphin-2.},
	url = {https://m2.mtmt.hu/api/publication/2085025},
	author = {Borics, Attila and Mallareddy, Jayapelreddy and Timári, István and E Kövér, Katalin and Keresztes, Attila and Tóth, Géza},
	doi = {10.1021/jm300836n},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {55},
	unique-id = {2085025},
	issn = {0022-2623},
	abstract = {Endomorphins (EM-1 and EM-2) are selective, high affinity agonists of the mu-opioid (MOP) receptor, an important target in pain regulation. Their clinical use is impeded by their poor metabolic stability and limited entry to the central nervous system. In this study, the Pro(2) residue of EM-2 was modified systematically through substitution by hydroxyproline (Hyp), (S)-beta-homoproline (betaPro), 2-aminocyclopentene-1-carboxylic acid (DeltaAcpc), or 2-aminocyclohexene-1-carboxylic acid (DeltaAchc) to obtain stable MOP active compounds. Both Hyp(2) and betaPro(2) substitution decreased receptor affinity. Analogues incorporating alicyclic beta-amino acids exhibited diverse receptor binding properties, depending on the configuration of the substituent side-chain. (1S,2R)DeltaAcpc(2)-EM-2 was shown to have MOP affinity and selectivity comparable to those of EM-2 and proved to act as agonist while being resistant to proteolysis. NMR and molecular dynamics (MD) studies revealed that bent backbone structures are predominant in the most potent analogues, while their presence is less pronounced in ligands of lower receptor affinity.},
	year = {2012},
	eissn = {1520-4804},
	pages = {8418-8428}
}

@article{MTMT:2057815,
	title = {Characterization of antinociceptive potency of endomorphin-2 derivatives with unnatural amino acids in rats},
	url = {https://m2.mtmt.hu/api/publication/2057815},
	author = {Kovács, Gyula István and Petrovszki, Zita and Mallareddy, Jayapelreddy and Tóth, Géza and Benedek, György and Horváth, Gyöngyi},
	doi = {10.1556/APhysiol.99.2012.3.12},
	journal-iso = {ACTA PHYSIOL HUNG},
	journal = {ACTA PHYSIOLOGICA HUNGARICA},
	volume = {99},
	unique-id = {2057815},
	issn = {0231-424X},
	year = {2012},
	eissn = {1588-2683},
	pages = {353-363},
	orcid-numbers = {Benedek, György/0000-0002-5066-6594; Horváth, Gyöngyi/0000-0002-6025-4577}
}

@article{MTMT:25394995,
	title = {Endomorphins: potential roles and therapeutic indications in the development of opioid peptide analgesic drugs},
	url = {https://m2.mtmt.hu/api/publication/25394995},
	author = {Liu, Wei X and Wang, Rui},
	doi = {10.1002/med.20222},
	journal-iso = {MED RES REV},
	journal = {MEDICINAL RESEARCH REVIEWS},
	volume = {32},
	unique-id = {25394995},
	issn = {0198-6325},
	year = {2012},
	eissn = {1098-1128},
	pages = {536-580}
}

@article{MTMT:1921998,
	title = {Transport Characteristics of Endomorphin-2 Analogues in Brain Capillary Endothelial Cells.},
	url = {https://m2.mtmt.hu/api/publication/1921998},
	author = {Mallareddy, Jayapelreddy and Tóth, Géza and Fazakas, Csilla and Molnár, Judit and Nagyőszi, Péter and Lipkowski, AW and Krizbai, István Adorján and Wilhelm, Imola Mária},
	doi = {10.1111/j.1747-0285.2011.01306.x},
	journal-iso = {CHEM BIOL DRUG DES},
	journal = {CHEMICAL BIOLOGY & DRUG DESIGN},
	volume = {79},
	unique-id = {1921998},
	issn = {1747-0277},
	abstract = {Due to their poor metabolic stability and limited blood-brain barrier (BBB) permeability, endomorphins (EMs) have a low analgesic efficacy when administered systemically. Therefore, it is of great importance to design analogues with improved peptidase resistance and better delivery to the central nervous system. Recently, novel endomorphin-2 (EM-2) analogues have been synthesized, which proved to bind with high affinity and selectivity to the mu-opioid receptors, and showed proteolytic resistance. In this study we have analyzed the transport characteristics of EM-2 and three of its analogues (Dmt-Pro-Phe-Phe-NH(2) , Tyr-(1S,2R)Acpc-Phe-Phe-NH(2) and Tyr-(1S,2R)Achc-Phe-Phe-NH(2) ) using an in vitro BBB model. The lipohilicity of the analogues, as assessed by their octanol/water partition coefficients, was higher than that of EM-2. The flux of all four peptides from the apical (blood) side to the basolateral (brain) side was not saturable in the 10 nM to 1 mM concentration range, suggesting that a passive mechanism plays a major role in their transport. The permeability coefficient of the analogues was significantly higher than that of EM-2, suggesting increased BBB penetration properties. We conclude that due to their good peptidase resistance and improved transport through brain endothelial cells these EM-2 analogues will have better analgesic properties in vivo. (c) 2011 John Wiley & Sons A/S.},
	year = {2012},
	eissn = {1747-0285},
	pages = {507-513},
	orcid-numbers = {Fazakas, Csilla/0000-0001-7822-5881; Wilhelm, Imola Mária/0000-0003-2366-7337}
}

@article{MTMT:2057724,
	title = {Stereoselective analysis of endomorphin diastereomers: Resolution of biologically active analogues by capillary electrophoresis applying cyclodextrins as mobile phase additives.},
	url = {https://m2.mtmt.hu/api/publication/2057724},
	author = {Németh, Krisztina and Mallareddy, Jayapelreddy and Domonkos, Celesztina Diána and Benéné Visy, Júlia and Tóth, Géza and Péter, Antal},
	doi = {10.1016/j.jpba.2012.05.013},
	journal-iso = {J PHARMACEUT BIOMED ANAL},
	journal = {JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS},
	volume = {70},
	unique-id = {2057724},
	issn = {0731-7085},
	abstract = {Seven diastereomer pairs of tetrapeptide analogues (TP) of endomorphin-1 and -2 were synthesized. A stereoselective capillary electrophoretic method was developed for controlling stereoisomeric ratio or purity. The isoelectric points of the tetrapeptides were between 8.3 and 8.9 as predicted and measured. A few of the analytes could be resolved without selectors due to the difference in their mobility. Neutral and anionic cyclodextrins (CDs) were applied in order to improve resolution. Stability constants as well as the mobilities of complexes were determined. Contributions of differences in the mobilities of free analytes and in the mobilities and stabilities of their complexes formed by CDs were equally important in the efficient resolution and migration order of diastereomers. As a result of the optimization of the pH of buffers and the concentration of the CD derivatives each diastereomer pair was resolved at baseline at least or better.},
	year = {2012},
	eissn = {1873-264X},
	pages = {32-39}
}

@article{MTMT:1955479,
	title = {Highly Efficient 1,4-Addition of Aldehydes to Nitroolefins: Organocatalysis in Continuous Flow by Solid-Supported Peptidic Catalysts},
	url = {https://m2.mtmt.hu/api/publication/1955479},
	author = {Ötvös, Sándor Balázs and Mándity, István and Fülöp, Ferenc},
	doi = {10.1002/cssc.201100332},
	journal-iso = {CHEMSUSCHEM},
	journal = {CHEMSUSCHEM},
	volume = {5},
	unique-id = {1955479},
	issn = {1864-5631},
	keywords = {PEPTIDES; AMINO-ACIDS; IMMOBILIZATION; ORGANIC-SYNTHESIS; Chemistry; organocatalysis; CONJUGATE ADDITION; Michael addition; CONTINUOUS FLOW REACTORS; REACTORS; AMINOCATALYSIS; MANNICH REACTIONS; GAMMA(2)-AMINO ACIDS; ASYMMETRIC ALDOL REACTIONS},
	year = {2012},
	eissn = {1864-564X},
	pages = {266-269},
	orcid-numbers = {Ötvös, Sándor Balázs/0000-0001-6673-1744; Mándity, István/0000-0003-2865-6143; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:23457877,
	title = {TAPP analogs containing beta(3)-homo-amino acids: synthesis and receptor binding},
	url = {https://m2.mtmt.hu/api/publication/23457877},
	author = {Podwysocka, D and Kosson, P and Lipkowski, AW and Olma, A},
	doi = {10.1002/psc.2433},
	journal-iso = {J PEPT SCI},
	journal = {JOURNAL OF PEPTIDE SCIENCE},
	volume = {18},
	unique-id = {23457877},
	issn = {1075-2617},
	year = {2012},
	eissn = {1099-1387},
	pages = {556-559}
}

@article{MTMT:22489896,
	title = {Conformation and chiral effects in α,β,α-tripeptides},
	url = {https://m2.mtmt.hu/api/publication/22489896},
	author = {Saavedra, CJ and Boto, A and Hernández, R and Miranda, JI and Aizpurua, JM},
	doi = {10.1021/jo300892u},
	journal-iso = {J ORG CHEM},
	journal = {JOURNAL OF ORGANIC CHEMISTRY},
	volume = {77},
	unique-id = {22489896},
	issn = {0022-3263},
	year = {2012},
	eissn = {1520-6904},
	pages = {5907-5913}
}

@article{MTMT:2057817,
	title = {Radiotracers, tritium labelling of neuropeptides},
	url = {https://m2.mtmt.hu/api/publication/2057817},
	author = {Tóth, Géza and Mallareddy, Jayapelreddy and Tóth, Fanni and Lipkowski, AW and Tourwe, D},
	doi = {10.3998/ark.5550190.0013.515},
	journal-iso = {ARKIVOC},
	journal = {ARKIVOC},
	volume = {2012},
	unique-id = {2057817},
	issn = {1551-7012},
	year = {2012},
	eissn = {1551-7004},
	pages = {163-174}
}

@article{MTMT:24537009,
	title = {A New Class of Highly Potent and Selective Endomorphin-1 Analogues Containing alpha-Methylene-beta-aminopropanoic Acids (Map)},
	url = {https://m2.mtmt.hu/api/publication/24537009},
	author = {Wang, Y and Xing, YH and Liu, X and Ji, H and Kai, M and Chen, ZY and Yu, J and Zhao, DP and Ren, H and Wang, R},
	doi = {10.1021/jm300664y},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {55},
	unique-id = {24537009},
	issn = {0022-2623},
	year = {2012},
	eissn = {1520-4804},
	pages = {6224-6236}
}

@article{MTMT:1868184,
	title = {Pharmacology of a new tritiated endomorphin-2 analog containing the proline mimetic cis-2-aminocyclohexanecarboxylic acid},
	url = {https://m2.mtmt.hu/api/publication/1868184},
	author = {Keresztes, Attila and Birkás, Erika and Pahi, A and Tóth, Géza and Bakota, L and Gulya, Károly and Szűcs, Mária},
	doi = {10.1016/j.peptides.2011.01.017},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {32},
	unique-id = {1868184},
	issn = {0196-9781},
	abstract = {As part of ongoing work aimed at generating proteolytically stable, readily applicable, radiolabeled endomorphin-2 (EM-2) analogs for elucidation of the topological requirements of peptide binding to mu-opioid receptors, we report here on the synthesis, radiolabeling, binding kinetics and binding site distribution of an EM-2 analog in which Pro(2) is replaced by 2-aminocyclohexanecarboxylic acid, ACHC. [H-3][(1S,2R)ACHC](EM)-E-2-2 (specific activity 63.49 Ci x mmol(-1)) bound specifically to its binding sites with high affinity (K-D = 0.55 +/- 0.06 nM) and saturably, yielding a receptor density, B-max of 151 +/- 4 fmol x mg protein(-1) in rat brain membranes. A similar affinity value was obtained in kinetic assays. Both Na+ and Gpp(NH)p decreased the affinity, proving the agonist character of the radioligand. Specific mu-opioid ligands displaced the radioligand with much higher affinities than did delta- and kappa-ligands. The autoradiographic distribution of the binding sites of [H-3][(1S,2R)ACHC](EM)-E-2-2 agreed well with the known locations of the mu-opioid receptors in the rat brain. In consequence of its high affinity, selectivity and enzymatic resistance [19], the new radioligand will be a good tool in studies of the topographical requirements of mu-opioid-specific peptide binding. (C) 2011 Elsevier Inc. All rights reserved.},
	year = {2011},
	eissn = {1873-5169},
	pages = {722-728}
}

@article{MTMT:1921580,
	title = {Design, Synthesis, Pharmacological Evaluation, and Structure-Activity Study of Novel Endomorphin Analogues with Multiple Structural Modifications},
	url = {https://m2.mtmt.hu/api/publication/1921580},
	author = {Mallareddy, Jayapelreddy and Borics, Attila and Keresztes, Attila and E Kövér, Katalin and Tourwe, D and Tóth, Géza},
	doi = {10.1021/jm101515v},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {54},
	unique-id = {1921580},
	issn = {0022-2623},
	abstract = {This study reports on new proteolytically stable, pharmacologically active endomorphin analogues, incorporating Dmt(1), Achc(2), pFPhe(4), or beta MePhe(4) unnatural amino acids. Consistent with earlier results, it was found that the analogues carrying anti and Achc2 residues displayed the highest p-opioid receptor affinities, depending upon the configuration of the incorporated Achc(2). Combination of such derivatives with pFPhe(4) or beta MePhe(4) yielded further compounds with variable binding potencies. Combined application of Dmt(1), cis-(1S,2R)Achc(2), and pFPhe(4) (compound 16) resulted in the most potent analogue. Ligand stimulated [S-35]GTP gamma S binding assays indicated that the analogues retained their agonist activities and opioid receptor specificities. NMR and molecular modeling studies of the analogues containing beta MePhe(4) or pFPhe(4) confirmed the predominance of bent structures, however, it is apparent that bent structures are energetically more favored than random/extended structures for all studied compounds.},
	keywords = {RAT-BRAIN; BIOLOGICAL-ACTIVITY; MU-OPIOID RECEPTORS; COUPLING-CONSTANTS; enzymatic degradation; alpha-amino acids; nuclear magnetic resonance; DIPEPTIDYL-PEPTIDASE IV; ENDOGENOUS OPIATES; BIOACTIVE CONFORMATION},
	year = {2011},
	eissn = {1520-4804},
	pages = {1462-1472}
}

@article{MTMT:1761918,
	title = {Az NMR spektroszkópia 40 éve Debrecenben. 40 years of NMR at the Department of Chemistry, University of Debrecen},
	url = {https://m2.mtmt.hu/api/publication/1761918},
	author = {Szilágyi, László and E Kövér, Katalin and Batta, Gyula and Bányai, István and Tóth, Imre},
	journal-iso = {MAGY KÉM FOLY KÉM KÖZL},
	journal = {MAGYAR KÉMIAI FOLYÓIRAT - KÉMIAI KÖZLEMÉNYEK (1997-)},
	volume = {117},
	unique-id = {1761918},
	issn = {1418-9933},
	year = {2011},
	eissn = {1418-8600},
	pages = {133-141},
	orcid-numbers = {Batta, Gyula/0000-0002-0442-1828; Bányai, István/0000-0002-6260-9175; Tóth, Imre/0000-0001-6718-9977}
}

@article{MTMT:1921985,
	title = {Asymmetric Synthesis and Conformational Analysis by NMR Spectroscopy and MD of Aba- and alpha-MeAba-Containing Dermorphin Analogues},
	url = {https://m2.mtmt.hu/api/publication/1921985},
	author = {Vandormael, B and De Wachter, R and Martins, JC and Hendrickx, PMS and Keresztes, Attila and Ballet, S and Mallareddy, Jayapelreddy and Tóth, Fanni and Tóth, Géza and Tourwe, D},
	doi = {10.1002/cmdc.201100314},
	journal-iso = {CHEMMEDCHEM},
	journal = {CHEMMEDCHEM},
	volume = {6},
	unique-id = {1921985},
	issn = {1860-7179},
	abstract = {Dermorphin analogues, containing a (S)- and (R)-4-amino1,2,4,5-tetrahydro-2-benzazepin-3-one scaffold (Aba) and the alpha-methylated analogues as conformationally constrained phenylalanines, were prepared. Asymmetric phase-transfer catalysis was unable to provide the (S)-alpha-Me-o-cyanophenylalanine precursor for (S)-alpha-MeAba in acceptable enantiomeric purity. However, by using a Schollkopf chiral auxiliary, this intermediate was obtained in 88% ee. [(S)-Aba 3-Gly 4] dermorphin retained mu-opioid affinity but displayed an increased delta-affinity. The corresponding R epimer was considerably less potent. In contrast, the [(R)-alpha-MeAba3-Gly4] dermorphin isomer was more potent than its S epimer. Tar-MD simulations of both non-methylated [Aba 3-Gly 4] dermorphin analogues showed a degree of folding at the C-terminal residues toward the N terminus of the peptide, without however, adopting a stabilized beta-turn conformation. The alpha-methylated analogues, on the other hand, exhibited a type I/I' beta-turn conformation over the alpha-MeAba3 and Gly4 residues, which was stabilized by a hydrogen bond involving Tyr5-H(N) and D-Ala 2-CO.},
	year = {2011},
	eissn = {1860-7187},
	pages = {2035-2047}
}

@article{MTMT:1921000,
	title = {Structural comparison of mu-opioid receptor selective peptides confirmed four parameters of bioactivity},
	url = {https://m2.mtmt.hu/api/publication/1921000},
	author = {Borics, Attila and Tóth, Géza},
	doi = {10.1016/j.jmgm.2009.11.006},
	journal-iso = {J MOL GRAPH MODEL},
	journal = {JOURNAL OF MOLECULAR GRAPHICS AND MODELLING},
	volume = {28},
	unique-id = {1921000},
	issn = {1093-3263},
	abstract = {Structural determinants of binding to the mu-opioid receptor, an important target in analgesia, attract great scientific attention. Many natural and synthetic peptides and peptidomimetics were shown previously to bind to this receptor selectively but there is no consensus about the structure responsible for biological activity. No high resolution structure of this receptor is available and the binding site of ligands is not exactly known. However, mu-opioid ligands with similar affinity and selectivity should possess at least one common structural feature. Comparative structural analysis of such ligands, considering adequate representation of binding conditions, may reveal key features of bioactivity. In this study ten mu-opioid receptor ligands, DAMGC, Tyr-W-MIF-1, morphiceptin, endomorphin-1 and 2 and their analogues, possessing different affinity and selectivity, were examined using molecular dynamics. Conformational preference of these molecules was determined in H2O and DMSO along with structural properties previously proposed to be important for binding. Four of such structural requirements were confirmed to be important, providing a possible structural model of receptor binding. Simultaneous fulfillment of these requirements results most likely in high affinity binding to the mu-opioid receptor. (C) 2009 Elsevier Inc. All rights reserved.},
	year = {2010},
	eissn = {1873-4243},
	pages = {495-505}
}

@article{MTMT:1921178,
	title = {Recent advances in endomorphin engineering},
	url = {https://m2.mtmt.hu/api/publication/1921178},
	author = {Keresztes, Attila and Borics, Attila and Tóth, Géza},
	doi = {10.1002/cmdc.201000077},
	journal-iso = {CHEMMEDCHEM},
	journal = {CHEMMEDCHEM},
	volume = {5},
	unique-id = {1921178},
	issn = {1860-7179},
	abstract = {Recent statistics from the World Health Organization indicate that a high percentage of people worldwide suffer from a wide variety of acute or cancer-associated chronic pain. At present, with a few exceptions, the treatment of severe pain relies upon oral administration of the mu-opioid receptor-targeting opiate morphine and its surrogates under strict clinical control. In spite of the powerful in vivo efficacy of these drugs, their long-term use is limited by antinociceptive tolerance, physical dependence, and respiratory depression that evolve. As no analgesics with moderate side effect profiles are currently available for the therapy of different types of pain and stages of cancer, considerable efforts must be made in the search for opiate substitutes. Following the recognition that endogenous peptide ligands of the opioid receptors exert striking effects in various pain models, and with the recent advances in chemical synthesis methods, research interest has steadily moved toward peptide-based compounds as potential opioid analgesics. The endomorphins are an attractive set of endogenous opioid peptides that may meet the requirements of opioid-based pain management. By virtue of their excellent mu-opioid receptor labeling and favorable analgesic properties, these tetrapeptides have gained attention in recent years as potential lead compounds. The ever-increasing number of publications in this field strongly suggests that modified analogues of endomorphins could serve as potent substitutes for opiates, with a lower propensity to induce side effects. This review surveys the main results achieved over the past decade regarding the design, radiolabeling, pharmacological characterization, and structure-activity features of a large body of endomorphin derivatives.},
	year = {2010},
	eissn = {1860-7187},
	pages = {1176-1196}
}

@article{MTMT:33643106,
	title = {Update 1 of: Over One Hundred Peptide-Activated G Protein-Coupled Receptors Recognize Ligands with Turn Structure},
	url = {https://m2.mtmt.hu/api/publication/33643106},
	author = {Ruiz-Gomez, Gloria and Tyndall, Joel D. A. and Pfeiffer, Bernhard and Abbenante, Giovanni and Fairlie, David P.},
	doi = {10.1021/cr900344w},
	journal-iso = {CHEM REV},
	journal = {CHEMICAL REVIEWS},
	volume = {110},
	unique-id = {33643106},
	issn = {0009-2665},
	keywords = {VASOACTIVE-INTESTINAL-PEPTIDE; GENE-RELATED PEPTIDE; THYROTROPIN-RELEASING-HORMONE; FOLLICLE-STIMULATING-HORMONE; NUCLEAR-MAGNETIC-RESONANCE; MELANIN-CONCENTRATING HORMONE; AGOUTI-RELATED-PROTEIN; DEPENDENT INSULINOTROPIC POLYPEPTIDE; GASTRIC-INHIBITORY-POLYPEPTIDE},
	year = {2010},
	eissn = {1520-6890},
	pages = {PR1-PR41},
	orcid-numbers = {Tyndall, Joel D. A./0000-0003-0783-1635; Pfeiffer, Bernhard/0000-0002-6209-0705; Fairlie, David P./0000-0002-7856-8566}
}

@article{MTMT:22225305,
	title = {Synthesis and Evaluation of New Endomorphin-2 Analogues Containing (Z)-alpha,beta-Didehydrophenylalanine (Delta(Z)Phe) Residues},
	url = {https://m2.mtmt.hu/api/publication/22225305},
	author = {Torino, D and Mollica, A and Pinnen, F and Feliciani, F and Lucente, G and Fabrizi, G and Portalone, G and Davis, P and Lai, J and Ma, SW and Porreca, F and Hruby, VJ},
	doi = {10.1021/jm1001343},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {53},
	unique-id = {22225305},
	issn = {0022-2623},
	year = {2010},
	eissn = {1520-4804},
	pages = {4550-4554}
}

@article{MTMT:1738641,
	title = {Design, synthesis and biological evaluation of novel endomorphins with multiply structural modifications},
	url = {https://m2.mtmt.hu/api/publication/1738641},
	author = {Toth, G and Mallareddy, JR and Borics, A and E Kövér, Katalin and Keresztes, A},
	journal-iso = {J PEPT SCI},
	journal = {JOURNAL OF PEPTIDE SCIENCE},
	volume = {16},
	unique-id = {1738641},
	issn = {1075-2617},
	year = {2010},
	eissn = {1099-1387},
	pages = {161}
}

@article{MTMT:21162819,
	title = {Structural chemistry of peptides containing backbone expanded amino acid residues: Conformational features of β, γ, and hybrid peptides.},
	url = {https://m2.mtmt.hu/api/publication/21162819},
	author = {Vasudev, PG and Chatterjee, S and Shamala, N and Balaram, P},
	doi = {10.1021/cr100100x},
	journal-iso = {CHEM REV},
	journal = {CHEMICAL REVIEWS},
	volume = {111},
	unique-id = {21162819},
	issn = {0009-2665},
	year = {2010},
	eissn = {1520-6890},
	pages = {657-687}
}

@article{MTMT:26522143,
	title = {Endogenous opiates and behavior: 2008},
	url = {https://m2.mtmt.hu/api/publication/26522143},
	author = {Bodnar, Richard J},
	doi = {10.1016/j.peptides.2009.09.027},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {30},
	unique-id = {26522143},
	issn = {0196-9781},
	year = {2009},
	eissn = {1873-5169},
	pages = {2432-2479}
}

@article{MTMT:22217296,
	title = {Structural studies of position 2 modified endomorphin-2 analogs by nmr spectroscopy and molecular modeling},
	url = {https://m2.mtmt.hu/api/publication/22217296},
	author = {Janecka, A and Perlikowska, R and Gach, K and Fichna, J and Mazur, A and Kruszynski, R and Janecki, T and Jankowski, S},
	journal-iso = {POL J CHEM},
	journal = {POLISH JOURNAL OF CHEMISTRY},
	volume = {83},
	unique-id = {22217296},
	issn = {0137-5083},
	year = {2009},
	pages = {1293-1307}
}

@article{MTMT:1920710,
	title = {Biological activity of endomorphin and [dmt(1)] endomorphin analogs with six-membered proline surrogates in position 2},
	url = {https://m2.mtmt.hu/api/publication/1920710},
	author = {Perlikowska, R and Gach, K and Fichna, J and Tóth, Géza and Walkowiak, B and do-Rego, JC and Janecka, A},
	doi = {10.1016/j.bmc.2009.04.046},
	journal-iso = {BIOORGAN MED CHEM},
	journal = {BIOORGANIC & MEDICINAL CHEMISTRY},
	volume = {17},
	unique-id = {1920710},
	issn = {0968-0896},
	year = {2009},
	eissn = {1464-3391},
	pages = {3789-3794}
}

@article{MTMT:20685193,
	title = {Catalytic, one-pot synthesis of beta-amino acids from alpha-amino acids. preparation of alpha,beta-peptide derivatives},
	url = {https://m2.mtmt.hu/api/publication/20685193},
	author = {Saavedra, C and Hernandez, R and Boto, A and Alvarez, E},
	doi = {10.1021/jo9004487},
	journal-iso = {J ORG CHEM},
	journal = {JOURNAL OF ORGANIC CHEMISTRY},
	volume = {74},
	unique-id = {20685193},
	issn = {0022-3263},
	year = {2009},
	eissn = {1520-6904},
	pages = {4655-4665}
}

@article{MTMT:22217295,
	title = {Synthesis and evaluation of new endomorphin analogues modified at the pro(2) residue},
	url = {https://m2.mtmt.hu/api/publication/22217295},
	author = {Torino, D and Mollica, A and Pinnen, F and Lucente, G and Feliciani, F and Davis, P and Lai, J and Ma, SW and Porreca, F and Hruby, VJ},
	doi = {10.1016/j.bmcl.2009.06.008},
	journal-iso = {BIOORG MED CHEM LETT},
	journal = {BIOORGANIC & MEDICINAL CHEMISTRY LETTERS},
	volume = {19},
	unique-id = {22217295},
	issn = {0960-894X},
	year = {2009},
	eissn = {1464-3405},
	pages = {4115-4118}
}