期刊
BIOSENSORS & BIOELECTRONICS
卷 26, 期 5, 页码 2772-2775出版社
ELSEVIER ADVANCED TECHNOLOGY
DOI: 10.1016/j.bios.2010.10.038
关键词
Amyloid-beta peptides; Depsi-peptides; Polymerization kinetics; Fibril elongation; Surface plasmon resonance
类别
资金
- Banca Intesa San Paolo
A wide variety of human diseases are associated with the formation of highly organized protein aggregates termed amyloid fibrils, whose growth (elongation) is due to the assembly of the basic molecular units (monomers) in a sequential polymerization process. Surface plasmon resonance (SPR) technology has been proposed as a powerful approach to study in detail the fibril elongation of some amyloidogenic peptides. In particular, the injection of monomers over immobilized fibrils allows to follow in real time, and on a very short time-scale, the kinetics of fibril growth. In the present study we confirmed and extended this application of SPR to A beta(1-42), hampered till now by the very pronounced aggregation propensity of this peptide, involved in Alzheimer disease. We took advantage of a new synthetic strategy (depsi-peptide technique) which allows to obtain reliable seed-free solutions (monomers) as well as fibrils of A beta(1-42). SPR data were consistent with a dock-and-lock mechanism underlying A beta(1-42) elongation process. The setup of an assay monitoring the elongation kinetics is very useful for investigating potential anti-amyloidogenic compounds. Moreover, the possibility to reliably immobilize both A beta(1-42) monomers and fibrils allows to measure the binding affinities of putative ligands for these different species. The approach applied here to A beta(1-42) might well be also applied to the study of other fibrillogenic peptides/proteins or to the study of polymerization reactions in general. (c) 2010 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据