@article{MTMT:3008464,
	title = {Metal-Binding Ability of Leu-Enkephalin, Related Glycoconjugates and Peptidomimetics},
	url = {https://m2.mtmt.hu/api/publication/3008464},
	author = {Majer, Zsuzsanna (Deckerné) and Vass, Elemér and Roscic, Maja and Hollósi, Miklós and Horvat, Stefica and Jakas, Andreja},
	doi = {10.5562/cca2725},
	journal-iso = {CROAT CHEM ACTA},
	journal = {CROATICA CHEMICA ACTA},
	volume = {88},
	unique-id = {3008464},
	issn = {0011-1643},
	abstract = {Both the chemistry and consequences of the nonenzymatic reaction between reducing sugars and reactive amino groups of amino acids, peptides and proteins (known as the Maillard reaction), have received considerable attention in food and health science fields. This initial reaction results in Amadori and similar products formation, followed by degradation to advanced glycation end products (AGEs). It is well established that AGEs are associated with color and odor of thermally processed or stored food, as well as with pathogen products in a number of diseases. The model systems of early stage Maillard reaction products (MRP) were prepared between endogenous opioid peptide leucine enkephalin (1) and D-glucose/D-glucuronic acid. The complexation ability of prepared MRP with metal ions (Ca2+, Zn2+, Al3+, Pb2+ and Cu2+) was investigated and compared to the complexation ability of parent peptide using ECD and FTIR spectroscopic measurements.},
	year = {2015},
	eissn = {1334-417X},
	pages = {281-287},
	orcid-numbers = {Vass, Elemér/0000-0001-8898-3846}
}

@article{MTMT:2578298,
	title = {Comprehensive Chiroptical Study of Proline-Containing Diamide Compounds},
	url = {https://m2.mtmt.hu/api/publication/2578298},
	author = {Knapp, Krisztina Nóra and Gorecki, M and Frelek, J and Luboradzki, R and Hollósi, Miklós and Majer, Zsuzsanna (Deckerné) and Vass, Elemér},
	doi = {10.1002/chir.22305},
	journal-iso = {CHIRALITY},
	journal = {CHIRALITY: THE PHARMACOLOGICAL BIOLOGICAL AND CHEMICAL CONSEQUENCES OF MOLECULAR ASYMMETRY},
	volume = {26},
	unique-id = {2578298},
	issn = {0899-0042},
	abstract = {The continuously growing interest in the understanding of peptide folding led to the conformational investigation of methylamides of N-acetyl-amino acids as diamide models. Here we report the results of detailed conformational analysis on Ac-Pro-NHMe and Ac--HPro-NHMe diamides. These compounds were analyzed by experimental and computational methods, the conformational distributions obtained by Density Functional Theory (DFT) calculations for isolated and solvated diamide compounds are discussed. The conformational preference of proline-containing diamide compounds as a function of the ambience was observed by a number of chiroptical spectroscopic techniques, such as vibrational circular dichroism (VCD), electronic circular dichroism (ECD), Raman optical activity (ROA) spectroscopy, and additionally by single crystal X-ray diffraction analyses. Based on a comparison between Ac-Pro-NHMe and Ac--HPro-NHMe, one can conclude that due to the greater conformational freedom of the -HPro derivative, Ac--HPro-NHMe shows different behavior in solid- and solution-phase, as well. Ac--HPro-NHMe tends to form cis Ac--HPro amide conformation in water, dichloromethane, and acetonitrile in contrast to its -Pro analog. On the other hand, the crystal structure of the -HPro compound cannot be related to any of the conformers obtained in vacuum and solution while the X-ray structure of Ac-Pro-NHMe was identified as t(L)-, which is a trans Ac-Pro amide containing conformer also predominant in polar solvents. Chirality 26:228-242, 2014. (c) 2014 Wiley Periodicals, Inc.},
	keywords = {PEPTIDES; ANALOGS; CIRCULAR-DICHROISM SPECTRA; PROTEIN-STRUCTURE; conformational analysis; ACIDS; infrared spectroscopy; IR; Vibrational circular dichroism; ECD; Electronic circular dichroism; Conformational preferences; VCD; RAMAN OPTICAL-ACTIVITY; ROA; Raman optical activity},
	year = {2014},
	eissn = {1520-636X},
	pages = {228-242},
	orcid-numbers = {Vass, Elemér/0000-0001-8898-3846}
}

@article{MTMT:2465435,
	title = {Conformational properties of secondary amino acids: Replacement of pipecolic acid by N-methyl-L-alanine in efrapeptin C},
	url = {https://m2.mtmt.hu/api/publication/2465435},
	author = {Konar, AD and Vass, Elemér and Hollósi, Miklós and Majer, Zsuzsanna (Deckerné) and Grüber, G and Frese, K and Sewald, N},
	doi = {10.1002/cbdv.201300086},
	journal-iso = {CHEM BIODIVERS},
	journal = {CHEMISTRY & BIODIVERSITY},
	volume = {10},
	unique-id = {2465435},
	issn = {1612-1872},
	abstract = {The efrapeptins, a family of naturally occurring peptides with inhibitory activities against ATPases, contain several α,α-disubstituted α-amino acids such as α-aminoisobutyric acid (Aib) or isovaline (Iva) besides pipecolic acid (Pip), β-Ala, Leu, Gly, and a C-terminal heterocyclic residue. Secondary α-amino acids such as proline are known to stabilize discrete conformations in peptides. A similar influence is ascribed to N-alkyl α-amino acids. We synthesized two efrapeptin C analogs with replacement of Pip by N-methyl-L-alanine (MeAla) using a combination of solid- and solution-phase techniques in a fragment-condensation strategy to compare the conformational bias of both secondary amino acids. The solution conformation was investigated by vibrational circular dichroism (VCD) to probe whether the analogs adopt a 310-helical conformation. The MeAla-containing analogs [MeAla1,3]efrapeptin C and [MeAla1,3,11]efrapeptin C inhibit ATP hydrolysis by the A3B3 complex of A 1A0-ATP synthase from Methanosarcina mazei Gö1. Copyright © 2013 Verlag Helvetica Chimica Acta AG, Zürich.},
	keywords = {PEPTIDE; INHIBITORS; ARTICLE; HYDROLYSIS; amino acid substitution; Protein Conformation; unclassified drug; Adenosine Triphosphate; protein synthesis; Circular Dichroism; amino acid; complex formation; structure activity relation; adenosine triphosphatase; pipecolic acid; PEPTAIBIOTICS; Helical conformation; Methanosarcina mazei; n methyl levo alanine; Efrapeptin C; Alanine, N-methyl-},
	year = {2013},
	eissn = {1612-1880},
	pages = {942-951},
	orcid-numbers = {Vass, Elemér/0000-0001-8898-3846}
}

@article{MTMT:2382937,
	title = {Chelate Structure of a Dirhodium–Amino Acid Complex Identified by Chiroptical and NMR Spectroscopy},
	url = {https://m2.mtmt.hu/api/publication/2382937},
	author = {Majer, Zsuzsanna (Deckerné) and Szilvágyi, Gábor and László, Benedek and Csámpai, Antal and Hollósi, Miklós and Vass, Elemér},
	doi = {10.1002/ejic.201300057},
	journal-iso = {EUR J INORG CHEM},
	journal = {EUROPEAN JOURNAL OF INORGANIC CHEMISTRY},
	volume = {2013},
	unique-id = {2382937},
	issn = {1434-1948},
	year = {2013},
	eissn = {1099-0682},
	pages = {3020-3027},
	orcid-numbers = {Csámpai, Antal/0000-0003-2107-7309; Vass, Elemér/0000-0001-8898-3846}
}

@article{MTMT:2382936,
	title = {Dirhodium complexes: determination of absolute configuration by the exciton chirality method using VCD spectroscopy.},
	url = {https://m2.mtmt.hu/api/publication/2382936},
	author = {Szilvágyi, Gábor and Brem, B and Bati, G and Tölgyesi, László and Hollósi, Miklós and Vass, Elemér},
	doi = {10.1039/c3dt51567b},
	journal-iso = {J CHEM SOC DALTON TRANS},
	journal = {JOURNAL OF THE CHEMICAL SOCIETY-DALTON TRANSACTIONS},
	volume = {42},
	unique-id = {2382936},
	issn = {1472-7773},
	abstract = {Inherently chiral dinuclear rhodium complexes have been synthesized from the well-known dirhodium(ii)-acetate and chiral/achiral amino acids. These complexes have a twisted paddlewheel structure due to axial chirality. Chiral induction could be observed when the ligands were chiral, opposite to the case of achiral ligands, where a racemic mixture was formed. The racemic mixture was separated by chiral HPLC-ECD. The stereochemical properties of these complexes were determined by VCD spectroscopy supported by theoretical calculations at the DFT level. We present a simple route to determine the absolute configuration by an exciton chirality method using VCD spectroscopy.},
	year = {2013},
	pages = {13137-13144},
	orcid-numbers = {Vass, Elemér/0000-0001-8898-3846}
}

@article{MTMT:2711350,
	title = {Vibrational and chiroptical spectroscopic investigation on diamide peptide models},
	url = {https://m2.mtmt.hu/api/publication/2711350},
	author = {Knapp, Krisztina Nóra and Hollósi, Miklós and Vass, Elemér and Majer, Zsuzsanna (Deckerné)},
	journal-iso = {J PEPT SCI},
	journal = {JOURNAL OF PEPTIDE SCIENCE},
	volume = {18},
	unique-id = {2711350},
	issn = {1075-2617},
	year = {2012},
	eissn = {1099-1387},
	pages = {S173-S173},
	orcid-numbers = {Vass, Elemér/0000-0001-8898-3846}
}

@article{MTMT:2382940,
	title = {A VCD-spektroszkópia alkalmazása peptidek, peptidmimetikumok és királis átmenetifém-komplexek térszerkezetének felderítésében},
	url = {https://m2.mtmt.hu/api/publication/2382940},
	author = {Hollósi, Miklós and Knapp, Krisztina Nóra and Majer, Zsuzsanna (Deckerné) and Szilvágyi, Gábor and Vass, Elemér},
	journal-iso = {MAGY KÉM FOLY KÉM KÖZL},
	journal = {MAGYAR KÉMIAI FOLYÓIRAT - KÉMIAI KÖZLEMÉNYEK (1997-)},
	volume = {118},
	unique-id = {2382940},
	issn = {1418-9933},
	year = {2012},
	eissn = {1418-8600},
	pages = {145-150},
	orcid-numbers = {Vass, Elemér/0000-0001-8898-3846}
}

@article{MTMT:2018509,
	title = {Synthesis and Conformational Analysis of Efrapeptins},
	url = {https://m2.mtmt.hu/api/publication/2018509},
	author = {Weigelt, S and Huber, T and Hofmann, F and Jost, M and Ritzefeld, M and Luy, B and Freudenberger, C and Majer, Zsuzsanna (Deckerné) and Vass, Elemér and Greie, JC and Panella, L and Kaptein, B and Broxterman, QB and Kessler, H and Altendorf, K and Sewald, N and Hollósi, Miklós},
	doi = {10.1002/chem.201102134},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {18},
	unique-id = {2018509},
	issn = {0947-6539},
	abstract = {The efrapeptin family of peptide antibiotics produced by the fungus Tolypocladium niveum, and the neo-efrapeptins from the fungus Geotrichum candidumare inhibitors of F1-ATPase with promising antitumor, antimalaria, and insecticidal activity. They are rich in Ca-dialkyl amino acids (Aib, Iva, Acc) and contain one beta-alanine and several pipecolic acid residues. The C-terminus bears an unusual heterocyclic cationic cap. The efrapeptins CG and three analogues of efrapeptin C were synthesized using a-azido carboxylic acids as masked amino acid derivatives. All compounds display inhibitory activity toward F1-ATPase. The conformation in solution of the peptides was investigated with electronic CD spectroscopy, FT-IR spectroscopy, and VCD spectroscopy. All efrapeptins and most efrapeptin analogues were shown to adopt helical conformations in solution. In the case of efrapeptin C, VCD spectra proved that a 310-helix prevails. In addition, efrapeptin C was conformationally studied in detail with NMR and molecular modeling. Besides NOE distance restraints, residual dipolar couplings (RDC) observed upon partial alignment with stretched PDMS gels were used for the conformational analysis and confirmed the 310-helical conformation.},
	year = {2012},
	eissn = {1521-3765},
	pages = {478-487},
	orcid-numbers = {Vass, Elemér/0000-0001-8898-3846}
}

@article{MTMT:2284925,
	title = {FREEZING EFFECT ON CHIRALITY AMPLIFICATION OF L-ASPARAGINE BY CRYSTALLIZATION OF THE RACEMATE IN PREFERENTIAL CONDITION},
	url = {https://m2.mtmt.hu/api/publication/2284925},
	author = {Vajda, T and Hollósi, Miklós},
	journal-iso = {CRYOLETTERS},
	journal = {CRYOLETTERS},
	volume = {32},
	unique-id = {2284925},
	issn = {0143-2044},
	abstract = {The role of freezing in stereoselection by crystallization of a saturated DL-asparagine solution in preferential condition of L-asparagine, has been investigated. To this end, the L-asparagine excess obtained by crystallization and then kept of different lengths of time at -20 degrees C in frozen aqueous solution was analyzed. The samples of the yielded materials were derivatised according to Marfey's method (see text). These derivatives were traced and evaluated by RP-HPLC analysis. The relatively best effects appeared after a one day treatment, where the freezing induced asymmetry amplifications and it increased the L-enantiomer excess from 10 mol % to 34.9, 35.0 and 35.5 mol go, respectively. Here we provide the first example of the influence of freezing on chirality amplification by preferential crystallization. Also some speculations are made about the implications of our findings in the prebiotic events of L-amino acids.},
	keywords = {AMINO-ACIDS; CRYSTALLIZATION; freezing; asparagine; meteorite; N-CARBOXYANHYDRIDE OLIGOMERIZATION; prebiotic amino acids; chirality amplification},
	year = {2011},
	eissn = {1742-0644},
	pages = {447-450}
}

@article{MTMT:1504473,
	title = {Conformational Studies on Chiral Rhodium Complexes by ECD and VCD Spectroscopy},
	url = {https://m2.mtmt.hu/api/publication/1504473},
	author = {Szilvágyi, Gábor and Majer, Zsuzsanna (Deckerné) and Vass, Elemér and Hollósi, Miklós},
	doi = {10.1002/chir.20916},
	journal-iso = {CHIRALITY},
	journal = {CHIRALITY: THE PHARMACOLOGICAL BIOLOGICAL AND CHEMICAL CONSEQUENCES OF MOLECULAR ASYMMETRY},
	volume = {23},
	unique-id = {1504473},
	issn = {0899-0042},
	year = {2011},
	eissn = {1520-636X},
	pages = {294-299},
	orcid-numbers = {Vass, Elemér/0000-0001-8898-3846}
}