CONFORMATIONAL MAPPING OF AMYLOID PEPTIDES FROM THE PUTATIVE NEUROTOXIC 25-35 REGION

被引:22
|
作者
LACZKO, I
HOLLY, S
KONYA, Z
SOOS, K
VARGA, JL
HOLLOSI, M
PENKE, B
机构
[1] CENT RES INST CHEM, H-1525 BUDAPEST, HUNGARY
[2] SZENT GYORGYI MED UNIV, DEPT MED CHEM, H-6720 SZEGED, HUNGARY
[3] EOTVOS LORAND UNIV, DEPT ORGAN CHEM, H-1518 BUDAPEST, HUNGARY
关键词
D O I
10.1006/bbrc.1994.2638
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 secondary structure of amyloid beta A(25-35) and its deletion analogues was studied by circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy and molecular dynamics calculation. Data of our comparative CD and FTIR measurements in trifluoroethanol suggest that beta A(25-35)NH2 has a preferred beta-sheet conformation. Contrary to this beta A(31-35)NH2 tends to adopt a beta-turn conformation. Based on the comparable neurotoxic effect of beta A(25-35)NH2 and beta A(31-35)NH2 the neurotoxicity likely involves the same 31-35 core sequence and the ''biologically active conformation'' is a beta-turn rather than a beta-sheet structure. (C) 1994 Academic Press, Inc.
引用
收藏
页码:120 / 126
页数:7
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