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PEGylated amyloid peptide nanocontainer delivery and release system

Castelletto, V., McKendrick, J. E. ORCID:, Hamley, I. W. ORCID:, Olsson, U. and Cenker, C. (2010) PEGylated amyloid peptide nanocontainer delivery and release system. Langmuir, 26 (14). pp. 11624-11627. ISSN 0743-7463

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To link to this item DOI: 10.1021/la101806z


A micellar nanocontainer delivery and release system is designed on the basis of a peptide-polymer conjugate. The hybrid molecules self-assemble into micelles comprising a modified amyloid peptide core surrounded by a PEG corona. The modified amyloid peptide previously studied in our group forms helical ribbons based on a beta-sheet motif and contains beta-amino acids that are excluded from the beta-sheet structure, thus being potentially useful as fibrillization inhibitors. In the model peptide-PEG hybrid system studied, enzymatic degradation using alpha-chymotrypsin leads to selective cleavage close to the PEG-peptide linkage, break up of the micelles, and release of peptides in unassociated form. The release of monomeric peptide is useful because aggregation of the released peptide into beta-sheet amyloid fibrils is not observed. This concept has considerable potential in the targeted delivery of peptides for therapeutic applications.

Item Type:Article
Divisions:Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) > Mass Spectrometry (CAF)
Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:16477
Publisher:American Chemical Society

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