PEGylated amyloid peptide nanocontainer delivery and release system
| Autor: | Valeria Castelletto, Ian W. Hamley, Ulf Olsson, John E. Mckendrick, Celen Cenker |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Circular dichroism
Stereochemistry Peptide macromolecular substances Crystallography X-Ray Micelle Polyethylene Glycols chemistry.chemical_compound PEG ratio Scattering Small Angle Spectroscopy Fourier Transform Infrared Electrochemistry Chymotrypsin General Materials Science Amino Acid Sequence Peptide sequence Spectroscopy Micelles chemistry.chemical_classification Drug Carriers Amyloid beta-Peptides Circular Dichroism Nanocontainer Surfaces and Interfaces Condensed Matter Physics Peptide Fragments Nanostructures Monomer chemistry Biophysics Conjugate |
| Zdroj: | Langmuir : the ACS journal of surfaces and colloids. 26(14) |
| ISSN: | 1520-5827 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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