PEGylated Amyloid Peptide Nanocontainer Delivery and Release System

被引：54

作者：

Castelletto, V. ^{[1
]}

McKendrick, J. E. ^{[1
]}

Hamley, I. W. ^{[1
,3
]}

Olsson, U. ^{[2
]}

Cenker, C. ^{[2
]}

机构：

[1] Univ Reading, Dept Chem, Reading RG6 6AD, Berks, England

[2] Lund Univ, S-22100 Lund, Sweden

[3] Diamond Light Source, Didcot 0X11 0DE, Oxon, England

来源：

LANGMUIR | 2010年 / 26卷 / 14期

基金：

英国工程与自然科学研究理事会;

关键词：

PROTEIN; CONJUGATE; ACID;

D O I：

10.1021/la101806z

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：11624 / 11627

页数：4

共 35 条

[1] Helical-Ribbon Formation by a β-Amino Acid Modified Amyloid β-Peptide Fragment [J].