Resilin-like polypeptides (RLPs) are intrinsically disordered proteins (IDPs) that may undergo liquid-liquid phase separation (LLPS). The interactions between solvent molecules, ionic species that may be present in solution, and the functional groups of the amino acids in the peptide are key features that control their upper critical solution temperature (UCST). Acrylamide functionalities chemically attached to the RLPs alters the overall hydrophobicity of the polypeptide with an impact in the phase transition temperatures allowing the formation of hydrogels free of agents that may be non-biologically friendly. In addition, the acrylamide groups also permit photo-crosslinking that will arrest the intrinsic microstructure of the RLP emulsion formed due to the RLP phase separation. Identification of the appropriate polypeptide concentration and temperature gradient (from the soluble to insoluble regimes in the phase diagram) results in hydrogels with heterogeneous regions rich in polypeptides that can be used to guide cell localization in materials relevant for tissue engineering. These studies help us to understand the driving forces of LLPS in RLPs, so we can establish design parameters for making RLP-based hydrogels with controlled microstructure.

Effect of amino acid substitutions on the phase separation of resilin-like polypeptides: Applications in microstructured hydrogels

ACS Fall 2020 Virtual Meeting

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.