@article{MTMT:2868602,
	title = {Induced Folding of Protein-Sized Foldameric β-Sandwich Models with Core β-Amino Acid Residues},
	url = {https://m2.mtmt.hu/api/publication/2868602},
	author = {Olajos, Gábor and Hetényi, Anasztázia and Wéber, Edit and Németh, Lukács and Szakonyi, Zsolt and Fülöp, Ferenc and Martinek, Tamás},
	doi = {10.1002/chem.201405581},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {21},
	unique-id = {2868602},
	issn = {0947-6539},
	abstract = {The mimicry of protein-sized β-sheet structures with unnatural peptidic sequences (foldamers) is a considerable challenge. In this work, the de novo designed betabellin-14 β-sheet has been used as a template, and α→β residue mutations were carried out in the hydrophobic core (positions 12 and 19). β-Residues with diverse structural properties were utilized: Homologous β3-amino acids, (1R,2S)-2-aminocyclopentanecarboxylic acid (ACPC), (1R,2S)-2-aminocyclohexanecarboxylic acid (ACHC), (1R,2S)-2-aminocyclohex-3-enecarboxylic acid (ACEC), and (1S,2S,3R,5S)-2-amino-6,6-dimethylbicyclo[3.1.1]heptane-3-carboxylic acid (ABHC). Six α/β-peptidic chains were constructed in both monomeric and disulfide-linked dimeric forms. Structural studies based on circular dichroism spectroscopy, the analysis of NMR chemical shifts, and molecular dynamics simulations revealed that dimerization induced β-sheet formation in the 64-residue foldameric systems. Core replacement with (1R,2S)-ACHC was found to be unique among the β-amino acid building blocks studied because it was simultaneously able to maintain the interstrand hydrogen-bonding network and to fit sterically into the hydrophobic interior of the β-sandwich. The novel β-sandwich model containing 25% unnatural building blocks afforded protein-like thermal denaturation behavior. Dissolving sandwiches: A water-soluble β-sandwich has been constructed by using cyclic β-amino acids in the hydrophobic core (see figure). The structural stability is highly dependent on the side-chain, and the destructuring effects of the β-residues could be minimized by using (1R,2S)-2-aminocyclohexanecarboxylic acid. The β-sandwich displays protein-like thermal denaturation behavior.},
	keywords = {PROTEINS; STABILITY; Protein Folding; Chemical bonds; amino acids; PEPTIDOMIMETICS; DICHROISM; molecular dynamics; chemical analysis; DYES; Hydrophobicity; Hydrogen bonds; molecular dynamics simulations; CHAINS; circular dichroism spectroscopy; Structural stabilities; Protein Engineering; Thermal denaturations; Hydrogen bonding network; NMR chemical shifts; PROTEIN STRUCTURES},
	year = {2015},
	eissn = {1521-3765},
	pages = {6173-6180},
	orcid-numbers = {Olajos, Gábor/0000-0002-2479-4891; Hetényi, Anasztázia/0000-0001-8080-6992; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Zsolt/0000-0003-2432-8409; Fülöp, Ferenc/0000-0003-1066-5287; Martinek, Tamás/0000-0003-3168-8066}
}

@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:2603674,
	title = {Experimental evidence of fluid secretion of rabbit lacrimal gland duct epithelium},
	url = {https://m2.mtmt.hu/api/publication/2603674},
	author = {Katona, Máté and Vízvári, Eszter and Németh, Lukács and Facskó, Andrea and Venglovecz, Viktória and Rakonczay, Zoltán and Hegyi, Péter and Tóth-Molnár, Edit},
	doi = {10.1167/iovs.14-14025},
	journal-iso = {INVEST OPHTH VIS SCI},
	journal = {INVESTIGATIVE OPHTHALMOLOGY AND VISUAL SCIENCE},
	volume = {55},
	unique-id = {2603674},
	issn = {0146-0404},
	abstract = {Purpose. To investigate the osmotic water permeability of lacrimal gland (LG) duct epithelium by means of calculation of filtration permeability and to investigate LG ductal fluid secretion. Methods. Experiments were performed on isolated rabbit LG duct segments maintained in short term culture. Osmotically determined fluid movement or fluid secretion into the closed intraluminal space of cultured LG interlobular ducts was analyzed using video microscopic technique. Results. The end of the LG ducts sealed after overnight incubation forming a closed luminal space. For the calculation of osmotic water permeability, ducts were initially perfused with isotonic HEPES-buffered solution, and then with hypotonic HEPES-buffered solution. Filtration permeability was calculated from the initial slope of the relative volume increase. Secretory responses to carbachol or to forskolin stimulation were also investigated. Forskolin stimulation resulted in a rapid and sustained secretory response in both solutions. Forskolin-stimulated fluid secretion was completely inhibited by bumetanide both in HEPES-buffered and in HCO3-/CO2- buffered solutions, suggesting the central role of Na+-K+-2Cl- cotransporter type 1 (NKCC1). Administration of carbachol initiated a rapid but short secretory response in both HEPES buffered and in HCO3-/CO2 buffered solutions. Atropine completely abolished the carbachol-evoked fluid secretion. Conclusions. New method was introduced to investigate LG duct function. Water permeability of rabbit LG duct epithelium was measured by calculating filtration permeability. Fluid secretion of LG duct cells induced by carbachol or forskolin was also demonstrated. These results provide calculated values of lacrimal duct osmotic permeability and direct experimental evidence of LG duct fluid secretion.},
	year = {2014},
	eissn = {1552-5783},
	pages = {4360-4367},
	orcid-numbers = {Venglovecz, Viktória/0000-0002-2316-7247; Rakonczay, Zoltán/0000-0002-1499-3416; Hegyi, Péter/0000-0003-0399-7259; Tóth-Molnár, Edit/0000-0001-7989-1616}
}

@article{MTMT:2459240,
	title = {Foldameric α/β-Peptide Analogs of the β-Sheet-Forming Antiangiogenic Anginex: Structure and Bioactivity},
	url = {https://m2.mtmt.hu/api/publication/2459240},
	author = {Hegedüs, Zsófia and Wéber, Edit and Kriston-Pál, Éva and Makra, Ildikó and Czibula, Ágnes and Monostori, Éva and Martinek, Tamás},
	doi = {10.1021/ja408054f},
	journal-iso = {J AM CHEM SOC},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {135},
	unique-id = {2459240},
	issn = {0002-7863},
	abstract = {The principles of beta-sheet folding and design for alpha-peptidic sequences are well established, while those for sheet mimetics containing homologated amino acid building blocks are still under investigation. To reveal the structure-function relations of beta-amino-acid-containing foldamers, we followed a top-down approach to study a series of alpha/beta-peptidic analogs of anginex, a beta-sheet-forming antiangiogenic peptide. Eight anginex analogs were developed by systematic alpha --> beta(3) substitutions and analyzed by using NMR and CD spectroscopy. The foldamers retained the beta-sheet tendency, though with a decreased folding propensity. beta-Sheet formation could be induced by a micellar environment, similarly to that of the parent peptide. The destructuring effect was higher when the alpha --> beta(3) exchange was located in the beta-sheet core. Analysis of the beta-sheet stability versus substitution pattern and the local conformational bias of the bulky beta(3)V and beta(3)I residues revealed that a mismatch between the H-bonding preferences of the alpha- and beta-residues played a minor role in the structure-breaking effect. Temperature-dependent CD and NMR measurements showed that the hydrophobic stabilization was scaled-down for the alpha/beta-peptides. Analysis of the biological activity of the foldamer peptides showed that four anginex derivatives dose-dependently inhibited the proliferation of a mouse endothelial cell line. The alpha --> beta(3) substitution strategy applied in this work can be a useful approach to the construction of bioactive beta-sheet mimetics with a reduced aggregation tendency and improved pharmacokinetic properties.},
	year = {2013},
	eissn = {1520-5126},
	pages = {16578-16584},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Wéber, Edit/0000-0002-5904-0619; Czibula, Ágnes/0000-0003-4461-2773; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:2347492,
	title = {Foldameric β-H18/20P mixed helix stabilized by head-to-tail contacts: A way to higher-order structures Foldameric-H18/20P Mixed Helix Stabilized by Head-to-Tail Contacts: A Way to Higher-Order Structures},
	url = {https://m2.mtmt.hu/api/publication/2347492},
	author = {Szolnoki, Éva Tünde and Hetényi, Anasztázia and Mándity, István and Fülöp, Ferenc and Martinek, Tamás},
	doi = {10.1002/ejoc.201201633},
	journal-iso = {EUR J ORG CHEM},
	journal = {EUROPEAN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {2013},
	unique-id = {2347492},
	issn = {1434-193X},
	abstract = {Peptidic foldamers are known to exhibit increased diversity in the periodic secondary-structure space in comparison with their natural counterparts, but their higher-order self-organization has been studied less thoroughly. In theory, large-diameter peptide foldamer helices have the capability of self-recognition through axial helix-helix interactions (e.g., head-to-tail), but this phenomenon has previously been observed in only one instance. In this article we report on the discovery of the largest-diameter β-peptidic mixed helix to date, the H18/20P helix. Its formation is solvent-dependent and its folding occurs cooperatively through head-to-tail self-assembly in solution. These findings suggest that axial helix-helix interactions can serve as a new mode for the formation of tertiary/quaternary structures for peptide foldamers, which also show higher-order structural diversity than natural proteins. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.},
	keywords = {PEPTIDES; FOLDAMERS; Protein Folding; amino acids; self-assembly; helical structures},
	year = {2013},
	eissn = {1099-0690},
	pages = {3555-3559},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Mándity, István/0000-0003-2865-6143; Fülöp, Ferenc/0000-0003-1066-5287; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:1955481,
	title = {Stereoselective synthesis of pinane-type tridentate aminodiols and their application in the enantioselective addition of diethylzinc to benzaldehyde},
	url = {https://m2.mtmt.hu/api/publication/1955481},
	author = {Csillag, Kinga Karola and Németh, Lukács and Martinek, Tamás and Szakonyi, Zsolt and Fülöp, Ferenc},
	doi = {10.1016/j.tetasy.2012.01.020},
	journal-iso = {TETRAHEDRON ASYMMETR},
	journal = {TETRAHEDRON-ASYMMETRY},
	volume = {23},
	unique-id = {1955481},
	issn = {0957-4166},
	abstract = {A library of pinane-based aminodiols were prepared from commercially available (1R)-(-)-myrtenol (-)-1. Compound (-)-1 was transformed into ally! trichloroacetamide (+)-2 via the acetimidate, followed by the Overman rearrangement. In order obtain the aminodiol structure, (+)-2 was subjected to stereoselective dihydroxylation with OsO4, resulting in dihydroxy trichloroacetamide (+)-3. The trichloroacetyl group was removed from (+)-3 with aqueous HCl and the (1R,2R,3S,5R)-3-amino-2-hydroxymethyl-6,6-dimethylbicyclo[3.1.1]heptan-2-ol hydrochloride (-)-4 obtained was transformed to primary, secondary and tertiary aminodiols by reductive amination, N-alkylation of aminodiol (+)-9 and debenzylation of N-benzyl aminodiol (+)-10, respectively. In the reactions of (+)-9 and (+)-14 with formaldehyde, highly regioselective ring closure was observed. In contrast with earlier results, the aminodiols gave pinane-fused oxazolidines (+)-11 and (-)-15. The aminodiols and their oxazolidine derivatives 5-15 were applied as chiral catalysts in the enantioselective addition of diethylzinc to benzaldehyde. The best enantioselectivity was observed in the case of the N-benzyl-substituted derivative (+)-9. (C) 2012 Elsevier Ltd. All rights reserved.},
	keywords = {DIASTEREOSELECTIVE SYNTHESIS; DIALKYLZINC; Aldehydes; REDUCTION; REARRANGEMENT; KETONES; CHIRAL LIGANDS; ACID-DERIVATIVES; (+)-3-CARENE; ALCOHOL-PROMOTED ADDITION},
	year = {2012},
	eissn = {1362-511X},
	pages = {144-150},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Szakonyi, Zsolt/0000-0003-2432-8409; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1926671,
	title = {Unique α,β- and α,α,β,β-peptide foldamers based on cis-β-aminocyclopentanecarboxylic acid},
	url = {https://m2.mtmt.hu/api/publication/1926671},
	author = {Berlicki, Ł and Pilsl, L and Wéber, Edit and Mándity, István and Cabrele, C and Martinek, Tamás and Fülöp, Ferenc and Reiser, O},
	doi = {10.1002/anie.201107702},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {51},
	unique-id = {1926671},
	issn = {1433-7851},
	abstract = {Waterproof: cis-β-Aminocylopentanecarboxylic acid is a highly suitable building block for the synthesis of α,β- and α,α,β, β-peptides that have unique helical structures with high stability in methanol and aqueous media. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.},
	keywords = {PEPTIDES; METHANOL; FOLDAMERS; amino acids; helical structures; aqueous media; Building blockes; High stability; cis-pentacine; β-amino acids},
	year = {2012},
	eissn = {1521-3773},
	pages = {2208-2212},
	orcid-numbers = {Wéber, Edit/0000-0002-5904-0619; Mándity, István/0000-0003-2865-6143; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1842290,
	title = {Peptidic foldamers: ramping up diversity},
	url = {https://m2.mtmt.hu/api/publication/1842290},
	author = {Martinek, Tamás and Fülöp, Ferenc},
	doi = {10.1039/c1cs15097a},
	journal-iso = {CHEM SOC REV},
	journal = {CHEMICAL SOCIETY REVIEWS},
	volume = {41},
	unique-id = {1842290},
	issn = {0306-0012},
	abstract = {Non-natural folded polymers (foldamers) display considerable versatility, and the design of such molecules is of great current interest. In this respect, peptidic foldamers are perhaps the best-characterized systems, as they populate a number of residue-controlled secondary structures, which have found various biological applications and have also led to the creation of nanostructured materials. This critical review covers recent developments related to diverse building blocks and modern foldamer design principles, such as the stereochemical patterning methods. The recent achievements concerning tertiary/quaternary structures and the self-assembling foldameric nanostructures are also addressed (176 references).},
	keywords = {DE-NOVO DESIGN; BETA-AMINO ACIDS; PROTEINOGENIC SIDE-CHAINS; MODEL SYNTHETIC FOLDAMERS; GCN4 LEUCINE-ZIPPER; HYDROGEN-BONDED RINGS; PARALLEL SHEET STRUCTURE; MIXED ALPHA/BETA-PEPTIDES; HELICAL SECONDARY STRUCTURES; EFFECTIVE SIMULATION PROTOCOLS},
	year = {2012},
	eissn = {1460-4744},
	pages = {687-702},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1842289,
	title = {Self-association-driven transition of the β-peptidic H12 helix to the H18 helix},
	url = {https://m2.mtmt.hu/api/publication/1842289},
	author = {Szolnoki, Éva Tünde and Hetényi, Anasztázia and Martinek, Tamás and Szakonyi, Zsolt and Fülöp, Ferenc},
	doi = {10.1039/c1ob06627g},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {10},
	unique-id = {1842289},
	issn = {1477-0520},
	abstract = {Various patterns of foldameric oligomers formed by trans-ABHC ((1S,2S,3S, 5S)-2-amino-6,6-dimethylbicyclo-[3.3.1]heptane-3-carboxylic acid) and beta(3)-hSer residues were studied. NMR, ECD and molecular modelling demonstrated that octameric and nonameric sequences with multiple i-i+3 ABHC pair repulsions attain the beta-H18 helix in CD3OH. As a close relative of the alpha-helix, this helix type is stabilized by i-i+4 backbone H-bond interactions. The formation of the beta-H18 helix was found to be solvent-and concentration-dependent. Upon dilution, the beta-H18 -> beta-H12 helix transition was revealed by concentration-dependent ECD, DOSY-NMR and TEM measurements.},
	keywords = {SECONDARY STRUCTURE; CIRCULAR-DICHROISM; SIDE-CHAINS; ACID OLIGOMERS; QUATERNARY STRUCTURE; ALPHA/BETA-PEPTIDES; STRUCTURAL-CHARACTERIZATION; AMPHIPATHIC PEPTIDES; MEMBRANE ENVIRONMENT; HETEROGENEOUS BACKBONES},
	year = {2012},
	eissn = {1477-0539},
	pages = {255-259},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Martinek, Tamás/0000-0003-3168-8066; Szakonyi, Zsolt/0000-0003-2432-8409; Fülöp, Ferenc/0000-0003-1066-5287}
}