Conformational behavior of C alpha,alpha-diphenyl glycine: extended conformation in tripeptides containing consecutive D phi G residues.

Abstract:

:Recent studies on the conformational preferences of the Dphig (C(alpha,alpha)-diphenylglycine) residue showed that this C(alpha,alpha)-disubstituted glycine has a structural versatility. In fact, depending on the nature of the following or preceding residue, Dphig can assume either folded or extended conformations. We have carried out the analysis of the conformational preferences of the Dphig residue in tripeptides containing consecutive Dphig residues. The crystal structures of Z-Dphig-Dphig -Dphig-OMe (a; Z = benzyloxycarbonyl; OMe = methyl ester), Z-Aib-Dphig-Dphig-OMe (b; Aib = alpha-aminoisobutyric acid), and Z-Ac(3)c-Dphig-Dphig-OMe (c; Ac(3)c = alpha-amino-cyclopropan carboxylic acid), are here reported. The Dphig residues adopt the fully extended conformation in the three tripeptides examined. Together with our previous findings on Dphig containing peptides, the structures of the peptides here examined, indicate that the presence of adjacent Dphig residue in the sequence further stabilizes the extended conformation.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Pavone V,Lombardi A,Saviano M,De Simone G,Nastri F,Maglio O,Omote Y,Yamanaka Y,Yamada T

doi

10.1002/(SICI)1097-0282(200002)53:2<161::AID-BIP6>

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

161-8

issue

2

eissn

0006-3525

issn

1097-0282

pii

10.1002/(SICI)1097-0282(200002)53:2<161::AID-BIP6>

journal_volume

53

pub_type

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