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The Materials Science of Protein Aggregation

Published online by Cambridge University Press:  31 January 2011

D.L. Cox,
H. Lashuel,
K.Y.C. Lee and
R.R.P. Singh
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Abstract

Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer's, Parkinson's, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig's disease), Huntington's, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science.

Keywords

amyloid diseasescomplex adaptive matteremergent behaviorprion diseasesprotein aggregationprotofibrilsnanotubesnanowires

Information

Type
Research Article
Information
MRS Bulletin , Volume 30 , Issue 6: Complex Adaptive Matter: Emergent Phenomena in Materials , June 2005, pp. 452 - 457
Copyright
Copyright © Materials Research Society 2005

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