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Research article2012Peer reviewed

Inhibition of Amyloid Formation

Härd, Torleif; Lendel, Christofer

Abstract

Amyloid is aggregated protein in the form of insoluble fibrils. Amyloid deposition in human tissue-amyloidosis-is associated with a number of diseases including all common dementias and type II diabetes. Considerable progress has been made to understand the mechanisms leading to amyloid formation. It is, however, not yet clear by which mechanisms amyloid and protein aggregates formed on the path to amyloid are cytotoxic. Strategies to prevent protein aggregation and amyloid formation are nevertheless, in many cases, promising and even successful. This review covers research on intervention of amyloidosis and highlights several examples of how inhibition of protein aggregation and amyloid formation has been achieved in practice. For instance, rational design can provide drugs that stabilize a native folded state of a protein, protein engineering can provide new binding proteins that sequester monomeric peptides from aggregation, small molecules and peptides can be designed to block aggregation or direct it into non-cytotoxic paths, and monoclonal antibodies have been developed for therapies towards neurodegenerative diseases based on inhibition of amyloid formation and clearance. (c) 2012 Elsevier Ltd. All rights reserved.

Keywords

protein aggregation; amyloidosis; drug discovery; protein engineering; neurodegenerative disease

Published in

Journal of Molecular Biology
2012, volume: 421, number: 4-5, pages: 441-465
Publisher: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD

SLU Authors

  • Härd, Torleif

    • Department of Molecular Biology, Swedish University of Agricultural Sciences

  • Lendel, Christofer

    • Department of Molecular Biology, Swedish University of Agricultural Sciences

Global goals (SDG)

SDG3 Good health and well-being

UKÄ Subject classification

Pharmaceutical Biotechnology
Medical Biotechnology
Biochemistry and Molecular Biology

Publication identifier

  • DOI: https://doi.org/10.1016/j.jmb.2011.12.062

Permanent link to this page (URI)

https://res.slu.se/id/publ/40818