3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides

Autor:	Gangadhar J. Sanjayan, Rajesh G. Gonnade, Pattuparambil R. Rajamohanan, Rupesh L. Gawade, Tukaram S. Ingole, Amol S. Kotmale
Rok vydání:	2016
Předmět:	chemistry.chemical_classification Circular dichroism 010405 organic chemistry Peptide General Chemistry 010402 general chemistry 01 natural sciences Catalysis 0104 chemical sciences Amino acid Folding (chemistry) Crystallography Peptide backbone chemistry Materials Chemistry Peptide sequence
Zdroj:	New Journal of Chemistry. 40:9205-9210
ISSN:	1369-9261 1144-0546
DOI:	10.1039/c6nj01667g
Popis:	This paper describes the consequences of incorporating a constrained heterocyclic aromatic β-amino acid 3-aminothiophenecarboxylic acid (3-Atc) into peptides containing β-turn forming elements such as Pro-Gly motif and the effect on the secondary structural architecture of the entire peptide backbone. Conformational investigations of oligomers comprising an α,β,α peptide sequence were carried out by single-crystal X-ray diffraction, solution-state NMR, nOe-restrained MD simulation and circular dichroism studies. The results suggested that these peptide sequences assume helical architecture. The helical folding in the oligomers was found to be devoid of inter-residual H-bonding, instead found to be stabilized by a co-operative effect of 6-membered H-bonding within the 3-Atc unit and conformational restrictions of individual amino acids in the peptide backbone.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::8020bf670f22d3dcf690561aa837491a https://doi.org/10.1039/c6nj01667g Zobrazit plný text záznamu