RESEARCH ARTICLE


Short Peptides as Inhibitors of Amyloid Aggregation



Bradley Neddenriep, Anastasia Calciano, Daniel Conti, Erin Sauve, Marissa Paterson, Edward Bruno, David A. Moffet*
Department of Chemistry and Biochemistry Loyola Marymount University 1 LMU Drive Los Angeles, CA 90045, USA


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Creative Commons License
© 2011 Neddenriep et al.

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: (https://creativecommons.org/licenses/by/4.0/legalcode). This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

* Address correspondence to this author at the Department of Chemistry and Biochemistry Loyola Marymount University 1 LMU Drive Los Angeles, CA 90045, USA; Tel: 310-338-4400; Fax: 001-310-338-2905; E-mail: dmoffet@lmu.edu


Abstract

The misfolding and aggregation of proteins into amyloid has been linked to a variety of age-related diseases. Aggregation of proteins, such as Aβ in Alzheimer's disease and Islet Amyloid Polypeptide (IAPP, amylin) in type 2 diabetes, appears to lead to the formation of toxic assemblies. These assemblies range in size from small oligomers (2-8 proteins) to large fibrils (thousands of proteins). It remains unclear how these amyloidogenic proteins misfold and form toxic species, but growing evidence suggests that inhibiting the aggregation of these proteins could slow, if not prevent altogether, the progression of these diseases. We describe the use of small peptides (<43 amino acids) as inhibitors of amyloid- based aggregation. These peptides, often short complementary segments of the amyloid proteins, can be useful (i) for identifying the aggregation-prone regions of the amyloid proteins (ii) as models for drug discovery and (iii) as potential therapeutic agents themselves.

Keywords: Amyloid Inhibition, Peptide Libraries, ABeta, Amylin, IAPP.