Hydrophilic elastomeric biomaterials based on resilin-like polypeptides

Abstract

The production of complex, yet well defined materials offers many opportunities in regenerative medicine, in which the mechanical and biological properties of the matrix must meet stringent requirements. Here we report the recombinant production of modular polypeptidic materials, based on the highly resilient protein resilin, which are equipped with multiple biologically active domains. The recombinant materials exhibit useful mechanical and cell adhesion behavior.

Microstructured Elastomer‐PEG Hydrogels via Kinetic Capture of Aqueous Liquid–Liquid Phase Separation

“…The RLPs were expressed following procedures extensively employed in the Kiick laboratories56, 57, 58, 59 and were functionalized with acrylamide groups to facilitate the desired on‐demand photo‐crosslinking of microscale domains. Chemical modification of RLP with N‐acryloxysuccinimide (NHS‐Ac) via reaction of lysine residues yielded RLP‐Ac ( Figure 1 A) via the protocols detailed in the Experimental Section.…”

A Genetically Engineered Protein Responsive to Multiple Stimuli

“…The association and dissociation at the UCST is observed to Figure S3.3 in the Supporting Information). Whilst LCST behavior has been observed in many thermoresponsive synthetic polymers [1,5] and proteins including EMPs, [2,6] UCST behavior is not common. UCST behavior has been reported in complex multisystem interpenetrating networks [18] of poly(acrylamide) and poly(acrylic acid), polyzwitterions, [19] and in gelatin.…”

“…Protein engineering approaches to biomaterials design offer powerful strategies to overcome challenges and provide new opportunities in the design and rapid development of responsive biomaterials. [2,[6][7][8] Consequently, there is a significant paradigm shift in the design concept for new elastic biomaterials, from a synthesis-based approach to the utilization of dynamic structural motifs derived from extracellular matrix proteins. Responsive properties of the highly elastic protein elastin and elastin-mimetic proteins (EMPs) that exhibit tunable lower critical solution temperatures (LCST) have stimulated development of novel protein-based biomaterials.…”

“…They are considered to be elastic owing to the presence of b-turn structures, and their LCST behavior is related to hydrophobic interactions. [6] Gelatin (Gly-Pro-Pro or Gly-Pro-Hyp) demonstrates gelation (UCST) owing to intermolecular triple-helix formation related to strong hydrogen bonding. [11] In rec1-resilin, high concentrations of both polar and charged side chains exist; it is hydrophilic ( Figure S4.2 in the Supporting Information) and predominantly random-coil in structure (Figure 1).…”

Engineering materials from proteins

“…81 Because of its properties, resilin has attracted significant interest for engineering artificial protein analogues, and several minimal sequences have been developed. These are actively being investigated for the development of new biomaterials, 82 where the minimal sequences are able to produce hydrogels with a relatively high resilience. The relationship between design of the minimal sequence, material processing and crosslinking, and the resilience of the final hydrogel continues to be an area of ongoing research as emerging knowledge from studies of native resilins is transferred into the design of artificially engineered protein polymer analogues.…”