Identification of the importance of the secondary structure of Alzheimer's disease amyloid

被引:12
作者
Cavillon, F
Elhaddaoui, A
Alix, AJP
Turrell, S
Dauchez, M
机构
[1] UNIV SCI & TECH LILLE FLANDRES ARTOIS,LAB SPECTROCHIM INFRAROUGE & RAMAN,CNRS,UPR A 2631 L,F-59655 VILLENEUVE DASCQ,FRANCE
[2] CHRU,INSERM,U314,F-51092 REIMS,FRANCE
关键词
Alzheimer's disease amyloid; congo red; infrared spectroscopy; molecular modelling;
D O I
10.1016/S0022-2860(96)09673-1
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Studies on the nature of the interaction between the marker dye, Congo red and Alzheimer's amyloid protein have been continued. Band-decomposition methods used on the infrared spectra clarify the changes in the SO; spectral region which result from dye-protein interactions and confirm the implication of this group during fixation. In order to complete a model for the mechanism of fixation, macromolecular modelling techniques have been used to obtain optimal tertiary structures of amyloid peptides 1-28 and 1-43. Finally, docking calculations indicate that arginine-5 and lysine-16 might be key residues involved in an interaction between Congo red and amyloid proteins. (C) 1997 Elsevier Science B.V.
引用
收藏
页码:185 / 189
页数:5
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