Effect of methylene group insertions on the structural rigidity of Aib containing helices

Duley, Anju and Gowda, Vasantha and Ganjiwale, Anjali and Raghothama, Srinivasarao and Ramanathan, Gurunath (2015) Effect of methylene group insertions on the structural rigidity of Aib containing helices. In: BIOPOLYMERS, 104 (6). pp. 720-732.

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Abstract

Nonprotein amino acids are being extensively used in the design of synthetic peptides to create new structure mimics. In this study we report the effect of methylene group insertions in a heptapeptide Boc-Ala(1)-Leu(2)-Aib(3)-Xxx(4)-Ala(5)-Leu(6)-Aib(7)-OMe which nicely folds into a mixed 3(10)-/-helical structure when Xxx= Ala. Analogs of this peptide have been made and studied by replacing central Xxx(4) residue with Glycine (-residue), -Alanine (-la), -aminobutyric acid (Gaba), and epsilon-aminocaproic acid (epsilon-Aca). NMR and circular dichroism were used to study the solution structure of these peptides. Crystals of the peptides containing alanine, -la, and Gaba reveal that increasing the number of central methylene (-CH2-) groups introduces local perturbations even as the helical structure is retained. (c) 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 104: 720-732, 2015.

Item Type:	Journal Article
Publication:	BIOPOLYMERS
Publisher:	WILEY-BLACKWELL
Additional Information:	Copy right for this article belongs to the WILEY-BLACKWELL, 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
Keywords:	Aib containing helices; mixed 310-; - helices; -alanine (-la); -aminobutyric acid (Gaba); epsilon-aminocaproic acid (epsilon-Aca)
Department/Centre:	Division of Chemical Sciences > NMR Research Centre (Formerly Sophisticated Instruments Facility)
Date Deposited:	18 Feb 2016 06:23
Last Modified:	18 Feb 2016 06:23
URI:	http://eprints.iisc.ac.in/id/eprint/53258

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