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
Date PublishedSEP

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.

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