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Issue 11, 2016
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3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides

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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.

Graphical abstract: 3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides

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The article was received on 27 May 2016, accepted on 10 Sep 2016 and first published on 12 Sep 2016

Article type: Paper
DOI: 10.1039/C6NJ01667G
Citation: New J. Chem., 2016,40, 9205-9210
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    3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides

    T. S. Ingole, A. S. Kotmale, R. L. Gawade, R. G. Gonnade, P. R. Rajamohanan and G. J. Sanjayan, New J. Chem., 2016, 40, 9205
    DOI: 10.1039/C6NJ01667G

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