LINEAR OLIGOPEPTIDES .252. ALPHA,BETA-DEHYDRO-AMINO ACID RESIDUES IN THE DESIGN OF PEPTIDE STRUCTURES - MOLECULAR AND CRYSTAL-STRUCTURES OF 2 FOLDED DEHYDRO PEPTIDES

被引：32

作者：

BUSETTI, V ^{[1
]}

CRISMA, M ^{[1
]}

TONIOLO, C ^{[1
]}

SALVADORI, S ^{[1
]}

BALBONI, G ^{[1
]}

机构：

[1] UNIV FERRARA,DEPT PHARMACEUT SCI,I-44100 FERRARA,ITALY

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 1992年 / 14卷 / 01期

关键词：

BETA-BENDS; ALPHA; BETA-DEHYDRO-PEPTIDES; BETA-DEHYDRO-PHENYLALANINE; PEPTIDES; X-RAY DIFFRACTION;

D O I：

10.1016/S0141-8130(05)80015-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The molecular and crystal structures of two N-alpha-protected tripeptide amides, containing in the central position the alpha-beta-dehydro-amino acid residue DELTA-Phe (Z-configurational isomer), were determined by X-ray diffraction. While Z-Gly-DELTA-Phe(z)-L-Pro-NH2 is characterized in the crystal state by the presence of a type 1 beta-bend conformation (at the DELTA-Phe(z)-L-Pro sequence), Z-D-Ala-DELTA-Phe(z)-Gly-NH2 is folded into two consecutive beta-bends (type II' followed by type I), at the D-Ala-DELTA-Phe(z) and DELTA-Phe(z)-Gly sequences, respectively. In both cases the achiral DELTA-Phe(z) residue adopts a set of phi, psi angles typical of the right-handed helical conformation. The DELTA-Phe residue may be exploited to design aromatic peptides with preferred secondary structures.

引用

页码：23 / 28

页数：6