Protein misfolding and aggregation: Mechanism, factors and detection

被引：118

作者：

Chaturvedi, Sumit Kumar ^{[1
]}

Siddiqi, Mohammad Khursheed ^{[1
]}

Alam, Parvez ^{[1
]}

Khan, Rizwan Hasan ^{[1
]}

机构：

[1] Aligarh Muslim Univ, Interdisciplinary Biotechnol Unit, Aligarh 202002, Uttar Pradesh, India

来源：

PROCESS BIOCHEMISTRY | 2016年 / 51卷 / 09期

关键词：

Protein misfolding; Protein aggregation; Amyloid fibril; Diseases; COLONY-STIMULATING FACTOR; FORMATION IN-VITRO; FIBRIL FORMATION; AMYLOID FIBRILS; PHYSIOLOGICAL CONDITIONS; MOLECULAR CHAPERONES; ELECTRON-MICROSCOPY; ALZHEIMERS-DISEASE; QUALITY CONTROL; SERUM-ALBUMIN;

D O I：

10.1016/j.procbio.2016.05.015

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Amyloidogenic diseases are characterised by the formation of amyloid aggregates inside or outside the cell. Amyloid-associated human diseases include Alzheimer's disease, Parkinson's disease, prion diseases and type II diabetes. Currently, these diseases are incurable; thus, detailed insight into the mechanism of amyloid formation, deposition and inhibition is required to develop treatment strategies. Herein, we have described the mechanism of amyloidogenesis in detail highlighting the major events including the association of native monomers into higher-ordered fibrillar structures. A review of the modern technologies that aid characterisation of amyloid aggregates is also discussed. Further, we have described the factors influencing the microenvironment of protein, which in turn promotes amyloidosis. (C) 2016 Elsevier Ltd. All rights reserved.

引用

页码：1183 / 1192

页数：10

共 92 条

[1]

Effect of the Interaction of the Amyloid β (1-42) Peptide with Short Single-Stranded Synthetic Nucleotide Sequences: Morphological Characterization of the Inhibition of Fibrils Formation and Fibrils Disassembly [J].