通过在末端添加氨基酸残基单元对β-淀粉样肽原纤维形成产生的显著影响。

Drastic effects on fibril formation of amyloid-beta peptides by the addition of amino acid residue units to the termini.

作者信息

Asanomi Yuya, Kobayashi Yumiko, Sakai Hiroki, Masuda Takuya, Chen Xinjiang, Chuman Yoshiro, Uosaki Kohei, Sakaguchi Kazuyasu

机构信息

Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, N10, W8, Kita-ku, Sapporo 060-0810, Japan.

出版信息

Protein Pept Lett. 2010 Apr;17(4):458-63. doi: 10.2174/092986610790963618.

DOI:10.2174/092986610790963618

PMID:20044924

Abstract

We report that the addition of amino acids to the amyloid peptide dramatically affected the structure and the rate of formation of amyloid fibrils. The attachment of three lysines to Abeta(10-35) gave the formation of remarkably long fibrils, while three glutamates resulted in a faster formation rate of the fibrils.

摘要

我们报告称，向淀粉样肽中添加氨基酸会显著影响淀粉样纤维的结构和形成速率。将三个赖氨酸连接到β-淀粉样蛋白（10-35）上会形成非常长的纤维，而三个谷氨酸则会导致纤维的形成速率加快。