Journal
MACROMOLECULES
Volume 48, Issue 12, Pages 4183-4195Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.macromol.5b00431
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Funding
- Government of Russian Federation [074-U01]
- Russian Foundation for Basic Research [14-03-00372a]
- National Science Foundation [DMR-1309892, DMR-1436201]
- National Institutes of Health [P01-HL108808, 1UH2HL123645]
- Cystic Fibrosis Foundation
- NIH [R01GM61232, R01-EB001630]
- NSF Triangle MRSEC [DMR-1121107]
- Direct For Mathematical & Physical Scien
- Division Of Materials Research [1309892] Funding Source: National Science Foundation
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The self-assembly of synthetic diblock copolymers has been extensively studied experimentally and theoretically. In contrast, self-assembly of polypeptide diblock copolymers has so far been mostly studied experimentally. We discovered that the theory developed for synthetic diblock copolymer does not fully explain the self-assembly of elastin-like polypeptide diblock copolymers, leading us to generalize the theory to make it applicable for these polypeptides. We demonstrated that elastin-like polypeptide diblocks self-assemble into weak micelles with dense cores and almost unstretched coronas, a state not previously observed for synthetic diblock copolymers. Weak micelles form if the surface tension at the core corona interface is low compared to that expected of a micelle with a dense core. The predictions of the theory of weak micelles for the critical micelle temperature, hydrodynamic radius, and aggregation number of elastin-like polypeptide diblocks are in reasonable agreement with the experimentally measured values. The unique and unprecedented control of amphiphilicity in these recombinant peptide polymers reveals a new micellar state that has not been previously observed in synthetic diblock copolymer systems.
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