Journal Article

FZJ-2016-06508

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Advances in the Simulation of Protein Aggregation at the Atomistic Scale

Carballo-Pacheco, M. ; Strodel, B. (Corresponding author)FZJ*

2016
Soc. Washington, DC

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Please use a persistent id in citations: doi:10.1021/acs.jpcb.6b00059

Abstract: Protein aggregation into highly structured amyloid fibrils is associated with various diseases including Alzheimer’s disease, Parkinson’s disease, and type II diabetes. Amyloids can also have normal biological functions and, in the future, could be used as the basis for novel nanoscale materials. However, a full understanding of the physicochemical forces that drive protein aggregation is still lacking. Such understanding is crucial for the development of drugs that can effectively inhibit aberrant amyloid aggregation and for the directed design of functional amyloids. Atomistic simulations can help understand protein aggregation. In particular, atomistic simulations can be used to study the initial formation of toxic oligomers which are hard to characterize experimentally and to understand the difference in aggregation behavior between different amyloidogenic peptides. Here, we review the latest atomistic simulations of protein aggregation, concentrating on amyloidogenic protein fragments, and provide an outlook for the future in this field.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 553 - Physical Basis of Diseases (POF3-553) (POF3-553)

Appears in the scientific report 2016

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Database coverage:
; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; No Authors Fulltext ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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