Kinetics of protein fibril formation: Methods and mechanisms. Int J Biol Macromol 2017 Jul;100:3-10
Date
06/22/2016Pubmed ID
27327908DOI
10.1016/j.ijbiomac.2016.06.052Scopus ID
2-s2.0-84996899088 (requires institutional sign-in at Scopus site) 57 CitationsAbstract
Amyloid fibril formation is a self-assembly reaction induced by favourable conformational changes of proteins leading to a stable, structurally organized aggregates. The deposition of stable protein fibrils in organs and tissues results in many diseases which are generally referred as amyloidosis. Though different disease conditions originate from sequentially and structurally different proteins, their fibrillar forms share common structural features. In vitro, fibril structure and kinetic pathway are investigated by using spectroscopic (fluorescence, circular dichroism, crystallography and solid state-NMR) and microscopic techniques. The kinetics of fibril formation is analysed using different mechanisms to understand the microscopic processes involved in the fibrillation reaction. This review discusses the assumptions, mechanisms, and limitations of some of the widely applied kinetic equations. Understanding of these equations would help to quantify the effect of the different microscopic process on the overall fibrillation kinetics which could aid in designing appropriate molecules to intervene in the aggregation process at different stages.
Author List
Kumar EK, Haque N, Prabhu NPAuthor
Neshatul Haque Postdoctoral Researcher 4 in the Mellowes Center for Genomic Sciences and Precision Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AmyloidAnimals
Humans
Kinetics
Models, Molecular
Mutation
Protein Aggregates
Protein Conformation
