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Inhibition of amyloid formation.
2012 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 421, no 4-5, p. 441-65Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
Elsevier, 2012. Vol. 421, no 4-5, p. 441-65
Keywords [en]
protein aggregation; amyloidosis; drug discovery; protein engineering; neurodegenerative disease
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-206105DOI: 10.1016/j.jmb.2011.12.062ISI: 000308383800003PubMedID: 22244855Scopus ID: 2-s2.0-84863987464OAI: oai:DiVA.org:kth-206105DiVA, id: diva2:1091175
Note

QC 20170502

Available from: 2017-04-26 Created: 2017-04-26 Last updated: 2017-05-02Bibliographically approved

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