PEGylated amyloid peptide nanocontainer delivery and release system

Castelletto, V., McKendrick, J. E. ORCID: https://orcid.org/0000-0003-2275-0569, Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926, Olsson, U. and Cenker, C. (2010) PEGylated amyloid peptide nanocontainer delivery and release system. Langmuir, 26 (14). pp. 11624-11627. ISSN 0743-7463 doi: 10.1021/la101806z

Abstract/Summary

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.