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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Veröffentlicht in:	Macromolecular rapid communications. Jg. 40; H. 2; S. e1800467 - n/a
Hauptverfasser:	Wright, Daniel B., Thompson, Matthew P., Touve, Mollie A., Carlini, Andrea S., Gianneschi, Nathan C.
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Germany Wiley Subscription Services, Inc 01.01.2019
Schlagworte:	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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Abstract	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.
AbstractList	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. 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.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. 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.
Author	Carlini, Andrea S. Gianneschi, Nathan C. Thompson, Matthew P. Touve, Mollie A. Wright, Daniel B.
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Snippet	Open‐to‐air aqueous‐phase ring‐opening metathesis polymerization‐induced self‐assembly (ROMPISA) is reported for forming well‐defined peptide polymer... Open-to-air aqueous-phase ring-opening metathesis polymerization-induced self-assembly (ROMPISA) is reported for forming well-defined peptide polymer...
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SubjectTerms	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
Title	Enzyme‐Responsive Polymer Nanoparticles via Ring‐Opening Metathesis Polymerization‐Induced Self‐Assembly
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