HARNESSING D-AMINO ACIDS FOR PEPTIDE MOTIF DESIGNS - SYNTHESIS AND SOLUTION CONFORMATION OF BOC-D-GLU-ALA-GLY-LYS-NHME AND BOC-L-GLU-ALA-GLY-LYS-NHME

被引:0
|
作者
BOBDE, V
SASIDHAR, YU
DURANI, S
机构
[1] Indian Inst Technol, CTR BIOTECHNOL, BOMBAY 400076, MAHARASHTRA, INDIA
[2] INDIAN INST TECHNOL, DEPT CHEM, BOMBAY 400076, INDIA
关键词
BETA-TURNS; D-AMINO ACID; ELECTROSTATICALLY STABILIZED PEPTIDES; 3(10)-HELICAL CONFORMATION; HELIX DESIGN; SALT BRIDGES;
D O I
暂无
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
In examining the use of D-amino acids in designing specific peptide folding motifs, the tetrapeptide Boc-D-Glu-Ala-Gly-Lys-NHMe 1 and its analog 2 featuring L-Glu were synthesized for a comparison of their solution conformations by NMR spectroscopy. The temperature coefficients of amide proton resonances, NOE data, side-chain CH2 anisotropies and salt titration results suggest a weak type II reverse-turn conformation for peptide 2, and a tandem type II' turn-3(10)-helix conformation of appreciable conformational stability for peptide I in apolar solvents. The latter is of potential interest as the N-terminal helix cap that could support the design of longer 3(10) helices. Possible origins of appreciable difference in the conformational stabilities of the diastereomers are discussed. (C) Munksgaard 1994.
引用
收藏
页码:209 / 218
页数:10
相关论文
共 22 条