The structures of fibril aggregates of beta-amyloid peptide 1-40 upon addition of dihexanoylphosphatidylcholine

被引：0

作者：

Lin, TL ^{[1
]}

Huang, CL ^{[1
]}

Lin, CM ^{[1
]}

Lin, HN ^{[1
]}

机构：

[1] Natl Tsing Hua Univ, Dept Engn & Syst Sci, Hsinchu 30043, Taiwan

来源：

NANOTECH 2003, VOL 3 | 2003年

关键词：

amyloid peptide; fibril; AFM; dynamic light scattering;

D O I：

暂无

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：

The amyloid peptide 1-40 forms fibril aggregates having lengths larger than several microns and a diameter around several nanometers. The growth rate and the average length of the fibril can be tuned by adding amphiphilic molecules. In this study, we will show that the addition of dihexanoylphosphatidylcholine (diC(6)PC) can effectively reduce the growth rate of the amyloid fibrils and can be used to tune the average length of the amyloid fibrils The growth process was studied by using AFM and also dynamic light scattering.

引用

页码：516 / 518

页数：3

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