Location of stimuli-responsive peptide sequences within silk-elastinlike protein-based polymers affects nanostructure assembly and drug-polymer interactions.

ABSTRACT: Silk-elastinlike protein polymers (SELPs) self-assemble into nanostructures when designed with appropriate silk-to-elastin ratios. Here, we investigate the effect of insertion of a matrix metalloproteinase-responsive peptide sequence, GPQGIFGQ, into various locations within the SELP backbone on supramolecular self-assembly. Insertion of the hydrophilic, enzyme-degradable sequence into the elastin repeats allows the formation of dilution-stable nanostructures, while insertion into the hydrophobic silk motifs inhibited self-assembly. The SELP assemblies retained their lower critical solution temperature (LCST) thermal response, allowing up to eightfold volumetric changes due to temperature-induced size change. A model hydrophobic drug was incorporated into SELP nanoassemblies utilising a com

SUBMITTER: Isaacson KJ 

PROVIDER: S-EPMC7454231 | biostudies-literature | 2020 Aug-Sep

REPOSITORIES: biostudies-literature