PEGylated amyloid peptide nanocontainer delivery and release system
Castelletto, V., McKendrick, J. E., Hamley, I. W., Olsson, U. and Cenker, C. (2010) PEGylated amyloid peptide nanocontainer delivery and release system. Langmuir, 26 (14). pp. 11624-11627. ISSN 0743-7463
Full text not archived in this repository.
To link to this article 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.