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. 2013 Sep 20;15(18):4866-9.
doi: 10.1021/ol402248s. Epub 2013 Sep 3.

Unconstrained homooligomeric γ-peptides show high propensity for C14 helix formation

Krishnayan Basuroy  1 , Bhimareddy Dinesh, M B Madhusudana Reddy, Siddapa Chandrappa, Srinivasarao Raghothama, Narayanaswamy Shamala, Padmanabhan Balaram
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Unconstrained homooligomeric γ-peptides show high propensity for C14 helix formation

Krishnayan Basuroy et al. Org Lett. .

Abstract

Monosubstituted γ(4)-residues (γ(4)Leu, γ(4)Ile, and γ(4)Val) form helices even in short homooligomeric sequences. C14 helix formation is established by X-ray diffraction in homooligomeric (γ)n tetra-, hexa- and decapeptide sequences demonstrating the high propensity of γ residues, with proteinogenic side chains, to adopt locally folded conformations.

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