Biomacromolecules
Biomacromolecules
5 years ago

Micellar Self-Assembly of Recombinant Resilin-/Elastin-Like Block Copolypeptides

Micellar Self-Assembly of Recombinant Resilin-/Elastin-Like Block Copolypeptides
Michael Gradzielski, Felipe Garcia Quiroz, Ingo Hoffmann, Michael Dzuricky, Isaac Weitzhandler, Ashutosh Chilkoti
Reported here is the synthesis of perfectly sequence defined, monodisperse diblock copolypeptides of hydrophilic elastin-like and hydrophobic resilin-like polypeptide blocks and characterization of their self-assembly as a function of structural parameters by light scattering, cryo-TEM, and small-angle neutron scattering. A subset of these diblock copolypeptides exhibit lower critical solution temperature and upper critical solution temperature phase behavior and self-assemble into spherical or cylindrical micelles. Their morphologies are dictated by their chain length, degree of hydrophilicity, and hydrophilic weight fraction of the ELP block. We find that (1) independent of the length of the corona-forming ELP block there is a minimum threshold in the length of the RLP block below which self-assembly does not occur, but that once that threshold is crossed, (2) the RLP block length is a unique molecular parameter to independently tune self-assembly and (3) increasing the hydrophobicity of the corona-forming ELP drives a transition from spherical to cylindrical morphology. Unlike the self-assembly of purely ELP-based block copolymers, the self-assembly of RLP–ELPs can be understood by simple principles of polymer physics relating hydrophilic weight fraction and polymer–polymer and polymer–solvent interactions to micellar morphology, which is important as it provides a route for the de novo design of desired nanoscale morphologies from first principles.

Publisher URL: http://dx.doi.org/10.1021/acs.biomac.7b00589

DOI: 10.1021/acs.biomac.7b00589

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