Helical screw-sense preferences of peptides based on chiral, Cα-tetrasubstituted α-amino acids.

Abstract:

:The preferred helical screw senses of chiral α-amino acids with a C(α)-tetrasubstituted α-carbon atom, as determined in the crystal state by X-ray diffraction analyses on derivatives and peptides, are reviewed. This survey covers C(α)-methylated and C(α)-ethylated α-amino acids, as well as α-amino acids cyclized on the α-carbon, including those characterized by the combination of lack of chirality at the α-carbon with either side-chain or axial chirality. Although, in general, chiral C(α)-tetrasubstituted α-amino acids show a less pronounced bias toward a single helical screw sense than their proteinogenic (C(α)-trisubstituted) counterparts, our analysis highlights significant differences in terms of magnitude and direction of such a bias among the various sub-families of residues, and between individual amino acids within each sub-family as well. The experimental findings can be rationalized, at least in part, on the basis of steric considerations.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Crisma M,Toniolo C

doi

10.1002/bip.22581

subject

Has Abstract

pub_date

2015-01-01 00:00:00

pages

46-64

issue

1

eissn

0006-3525

issn

1097-0282

journal_volume

104

pub_type

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