Accessibility navigation


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

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

To link to this item 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.

Item Type:Article
Refereed:Yes
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

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation