3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides12. (26th September 2016)

• Record Type: Journal Article
• Authors: Ingole, Tukaram S.; Kotmale, Amol S.; Gawade, Rupesh L.; Gonnade, Rajesh G.; Rajamohanan, Pattuparambil R.; Sanjayan, Gangadhar J.
• Is Part Of: New journal of chemistry. Volume 40:Number 11(2016:Nov.)
• Page Start: 9205
• Page End: 9210
• Publication Date: 2016-09-26
• Subjects: Chemistry -- Periodicals; Chimie -- Périodiques; 540
• DOI: 10.1039/c6nj01667g
• Languages: English
• ISSNs: 1144-0546

Abstract

Abstract : This article demonstrates the consequences of incorporating a constrained β-amino acid into a peptide chain and its effect on conformation of oligomers. Abstract : 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.