Enzyme‐Responsive Polymer Nanoparticles via Ring‐Opening Metathesis Polymerization‐Induced Self‐Assembly

Open‐to‐air aqueous‐phase ring‐opening metathesis polymerization‐induced self‐assembly (ROMPISA) is reported for forming well‐defined peptide polymer nanoparticles at room temperature and with high solids concentrations (10 w/w%). For these materials, ROMPISA is shown to provide control over molecul...

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Vydáno v:Macromolecular rapid communications. Ročník 40; číslo 2; s. e1800467 - n/a
Hlavní autoři: Wright, Daniel B., Thompson, Matthew P., Touve, Mollie A., Carlini, Andrea S., Gianneschi, Nathan C.
Médium: Journal Article
Jazyk:angličtina
Vydáno: Germany Wiley Subscription Services, Inc 01.01.2019
Témata:
Amino Acid Sequence
Assembly
block copolymers
Chemistry Techniques, Synthetic - methods
Enzymes
Hydrophobic and Hydrophilic Interactions
Metathesis
Microscopy, Electron, Transmission
Molecular Weight
Nanoparticles
Nanoparticles - chemistry
Nanoparticles - ultrastructure
Peptides
Peptides - chemical synthesis
Peptides - chemistry
Peptides - metabolism
Polymerization
Polymers
Polymers - chemical synthesis
Polymers - chemistry
Polymers - metabolism
Protein Structure, Secondary
Proteolysis
ROMPISA
self‐assembly
Thermolysin
Thermolysin - metabolism
block copolymers
self-assembly
peptides
ROMPISA
ISSN:1022-1336, 1521-3927, 1521-3927
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Shrnutí:Open‐to‐air aqueous‐phase ring‐opening metathesis polymerization‐induced self‐assembly (ROMPISA) is reported for forming well‐defined peptide polymer nanoparticles at room temperature and with high solids concentrations (10 w/w%). For these materials, ROMPISA is shown to provide control over molecular weight with high conversion while open‐to‐air. Moreover, these peptide polymer nanoparticles can spontaneously rearrange into larger aggregate scaffolds in the presence of the proteolytic enzyme, thermolysin. This work demonstrates the robust nature of ROMPISA, highlighted here for the preparation of stimuli‐responsive nanostructures in one pot, in air. Peptide‐functionalized polymer nanoparticles, both spherical micelles and framboidal vesicles, are formed via ring‐opening metathesis polymerization‐induced self‐assembly. When incubated with protease, the peptides are cleaved and the particles undergo an in situ reorganization into large macromolecular aggregates.
Bibliografie:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:1022-1336
1521-3927
1521-3927
DOI:10.1002/marc.201800467