PEGylated amyloid peptide nanocontainer delivery and release system
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 hel...
Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 26(2010), 14 vom: 20. Juli, Seite 11624-7 |
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1. Verfasser: | |
Weitere Verfasser: | , , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2010
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Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Amyloid beta-Peptides Drug Carriers Micelles Peptide Fragments Polyethylene Glycols 3WJQ0SDW1A Chymotrypsin EC 3.4.21.1 |
Zusammenfassung: | 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 |
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Beschreibung: | Date Completed 01.12.2010 Date Revised 01.12.2018 published: Print Citation Status MEDLINE |
ISSN: | 1520-5827 |
DOI: | 10.1021/la101806z |