EFFECTS OF THE MUTATIONS GLU22 TO GLN AND ALA21 TO GLY ON THE AGGREGATION OF A SYNTHETIC FRAGMENT OF THE ALZHEIMERS AMYLOID-BETA A4 PEPTIDE

被引：81

作者：

CLEMENTS, A ^{[1
]}

WALSH, DM ^{[1
]}

WILLIAMS, CH ^{[1
]}

ALLSOP, D ^{[1
]}

机构：

[1] QUEENS UNIV BELFAST,CTR MED BIOL,SCH BIOL & BIOCHEM,DIV BIOCHEM,97 LISBURN RD,BELFAST BT9 7BL,ANTRIM,NORTH IRELAND

来源：

NEUROSCIENCE LETTERS | 1993年 / 161卷 / 01期

基金：

英国惠康基金;

关键词：

CEREBRAL AMYLOID ANGIOPATHY; ALZHEIMERS DISEASE; AMYLOID; BETA-A4; PROTEIN; SYNTHETIC PEPTIDE;

D O I：

10.1016/0304-3940(93)90129-9

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

We assessed the fibrillogenic properties of synthetic peptides corresponding to residues 13-26 of beta/A4 amyloid, containing either the normal sequence (beta13 26) or the mutations Glu 22 to Gln (beta13 26Q22) and Ala21 to Gly (beta13 26G21). The kinetics of aggregation were monitored at 37-degrees-C and pH 7.4 by measuring the amount of peptide remaining in solution, using reverse-phase high performance liquid chromatography. Negative stain electron microscopy revealed that all of the peptides formed fibrils. However, beta13 26Q22 showed greatly accelerated fibril formation compared to the other two. The results suggest that the Q22 mutation confers increased amyloidogenic properties on the beta/A4 peptide, whereas the G21 mutation acts by a different pathogenic mechanism.

引用

页码：17 / 20

页数：4

共 21 条

[1] EXACT CLEAVAGE SITE OF ALZHEIMER AMYLOID PRECURSOR IN NEURONAL PC-12 CELLS [J].