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

Krishnayan Basuroy; Bhimareddy Dinesh; M B Madhusudana Reddy; Siddapa Chandrappa; Srinivasarao Raghothama; Narayanaswamy Shamala; Padmanabhan Balaram

doi:10.1021/ol402248s

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

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

Authors

Krishnayan Basuroy¹, Bhimareddy Dinesh, M B Madhusudana Reddy, Siddapa Chandrappa, Srinivasarao Raghothama, Narayanaswamy Shamala, Padmanabhan Balaram

Affiliation

¹ Molecular Biophysics Unit, Department of Physics, Sophisticated Instrumentation Facility, Indian Institute of Science , Bangalore 560 012, India.

PMID: 24000950
DOI: 10.1021/ol402248s

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Crystallography, X-Ray
Models, Molecular*
Molecular Structure
Peptides / chemical synthesis
Peptides / chemistry*
Protein Conformation
Protein Structure, Secondary

Substances

Peptides