3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides
| Title | 3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides |
| Publication Type | Journal Article |
| Year of Publication | 2016 |
| Authors | Ingole, TS, Kotmale, AS, Gawade, RL, Gonnade, RG, Rajamohanan, PR, Sanjayan, GJ |
| Journal | New Journal of Chemistry |
| Volume | 40 |
| Issue | 11 |
| Pagination | 9205-9210 |
| Date Published | SEP |
| 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. |
| DOI | 10.1039/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
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