LINEAR OLIGOPEPTIDE .279. STRUCTURES OF PEPTIDES FROM ALPHA-AMINO-ACIDS METHYLATED AT THE ALPHA-CARBON

被引:240
作者
TONIOLO, C
CRISMA, M
FORMAGGIO, F
VALLE, G
CAVICCHIONI, G
PRECIGOUX, G
AUBRY, A
KAMPHUIS, J
机构
[1] UNIV FERRARA,DEPT PHARMACEUT SCI,I-44100 FERRARA,ITALY
[2] UNIV BORDEAUX 1,CRYSTALLOG & CRYSTALLINE PHYS LAB,F-33405 TALENCE,FRANCE
[3] UNIV NANCY 1,MINERAL & CRYSTALLOG LAB,F-54506 VANDOEUVRE NANCY,FRANCE
[4] DSM RES & PATENTS,BIOORGAN CHEM SECT,6160 MD GELEEN,NETHERLANDS
关键词
D O I
10.1002/bip.360330708
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 structural preferences of peptides (and depsipeptides) from the achiral MeAib and Hib residues, and the chiral Iva, (alphaMe)Val, (alphaMe)Leu, and (alphaMe)Phe residues, as determined by conformational energy computations, x-ray diffraction analyses, and H-1-nmr and spectroscopic studies, are reviewed and compared with literature data on Aib-containing peptides. The results obtained indicate that helical structures are preferentially adopted by peptides rich in these alpha-amino acids methylated at the alpha-carbon. Intriguing experimental findings on the impact of the chirality of Iva, (alphaMe) Val, and (alphaMe) Phe residues on helix screw sense are illustrated.
引用
收藏
页码:1061 / 1072
页数:12
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