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

Title3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides
Publication TypeJournal Article
Year of Publication2016
AuthorsIngole, TS, Kotmale, AS, Gawade, RL, Gonnade, RG, Rajamohanan, PR, Sanjayan, GJ
JournalNew Journal of Chemistry
Volume40
Issue11
Pagination9205-9210
Date PublishedSEP
Abstract

This paper describes the consequences of incorporating a constrained heterocyclic aromatic b-amino acid 3-aminothiophenecarboxylic acid (3-Atc) into peptides containing beta-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 alpha,beta,alpha 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.

DOI10.1039/c6nj01667g
Type of Journal (Indian or Foreign)

Foreign

Impact Factor (IF)

3.277

Divison category: 
Center for Material Characterization (CMC)
Central NMR Facility
Organic Chemistry