Elastin-like Polypeptide Diblock Copolymers Self-Assemble into Weak Micelles.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Hassouneh, W; Zhulina, EB; Chilkoti, A; Rubinstein, M

Published Date

  • June 11, 2015

Published In

Volume / Issue

  • 48 / 12

Start / End Page

  • 4183 - 4195

PubMed ID

  • 27065492

Pubmed Central ID

  • 27065492

Electronic International Standard Serial Number (EISSN)

  • 1520-5835

International Standard Serial Number (ISSN)

  • 0024-9297

Digital Object Identifier (DOI)

  • 10.1021/acs.macromol.5b00431

Language

  • eng