Journal
LANGMUIR
Volume 26, Issue 14, Pages 11624-11627Publisher
AMER CHEMICAL SOC
DOI: 10.1021/la101806z
Keywords
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Funding
- EPSRC [EP/F048114/1, EP/G026203/1]
- Engineering and Physical Sciences Research Council [EP/G026203/1, EP/F048114/1] Funding Source: researchfish
- EPSRC [EP/F048114/1, EP/G026203/1] Funding Source: UKRI
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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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