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PEGylated Amyloid Peptide Nanocontainer Delivery and Release System

Castelletto, V.; McKendrick, J. E.; Hamley, I. W.; Olsson, Ulf LU and Cenker, Celen LU (2010) In Langmuir 26(14). p.11624-11627
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
26
issue
14
pages
11624 - 11627
publisher
The American Chemical Society
external identifiers
  • wos:000279756700005
  • scopus:77956666229
ISSN
0743-7463
DOI
10.1021/la101806z
language
English
LU publication?
yes
id
08e889ca-594a-4d4b-9df0-2b1bff879263 (old id 1657397)
date added to LUP
2010-08-30 13:08:23
date last changed
2018-05-29 11:56:02
@article{08e889ca-594a-4d4b-9df0-2b1bff879263,
  abstract     = {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.},
  author       = {Castelletto, V. and McKendrick, J. E. and Hamley, I. W. and Olsson, Ulf and Cenker, Celen},
  issn         = {0743-7463},
  language     = {eng},
  number       = {14},
  pages        = {11624--11627},
  publisher    = {The American Chemical Society},
  series       = {Langmuir},
  title        = {PEGylated Amyloid Peptide Nanocontainer Delivery and Release System},
  url          = {http://dx.doi.org/10.1021/la101806z},
  volume       = {26},
  year         = {2010},
}