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

TitleElastin-like Polypeptide Diblock Copolymers Self-Assemble into Weak Micelles.
Publication TypeJournal Article
Year of Publication2015
AuthorsW Hassouneh, EB Zhulina, A Chilkoti, and M Rubinstein
JournalMacromolecules
Volume48
Issue12
Start Page4183
Pagination4183 - 4195
Date Published06/2015
Abstract

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.

DOI10.1021/acs.macromol.5b00431
Short TitleMacromolecules