Elastin‐Like Recombinamers: Deconstructing and Recapitulating the Functionality of Extracellular Matrix Proteins Using Recombinant Protein Polymers

Abstract

In the development of tissue engineering strategies to replace, remodel, regenerate, or support damaged tissue, the development of bioinspired biomaterials that recapitulate the physicochemical characteristics of the extracellular matrix has received increased attention. Given the compositional heterogeneity and tissue-to-tissue variation of the extracellular matrix, the design, choice of polymer, crosslinking, and nature of the resulting biomaterials are normally depended on intended application. Generally, these biomaterials are usually made of degradable or nondegradable biomaterials that can be used as cell or drug carriers. In recent years, efforts to endow reciprocal biomaterial-cell interaction properties in scaffolds have inspired controlled synthesis, derivatization, and functionalization of the polymers used. In this regard, elastin-like recombinant proteins have generated interest and continue to be developed further owing to their modular design at a molecular level. In this review, the authors provide a summary of key extracellular matrix features relevant to biomaterials design and discuss current approaches in the development of extracellular matrix-inspired elastin-like recombinant protein based biomaterials.

Charge Density as a Molecular Modulator of Nanostructuration in Intrinsically Disordered Protein Polymers

“…11 This recombinant synthesis enables the rational design of hierarchically assembled protein nanosystems, including micelles, vesicles and physical hydrogels, with potential application in biotechnology and materials engineering. 12,13 Electrostatic interactions between ionic amino acids are one of the parameters that mediate self-assembling of IDPs and IDPPs. [14][15][16] Indeed, the presence of ionic amino acids contribute to phase transition and folding of ELRs and ELR-based bioconjugates, 17,18 enabling the production of innovative supramolecular nanomaterials.…”

Recent developments in sustainably sourced protein-based biomaterials

“…Recombinant technology provides an alternative method to produce proteins that are not naturally available in abundant quantities, as well as to modify the properties of these recombinant proteins, for example, by adding other bioactive molecules, growth factors, cell-binding domains, or other direct chemical modifications [33,34]. There are many successful reports of using of recombinant proteins to develop protein-based biomaterials; however, issues relating to low yield and scalability hinder their widespread commercial adoption [35][36][37]. However, with increasing interest in cellular agriculture, these limitations may soon be overcome.…”

Harnessing biomolecules for bioinspired dental biomaterials

“…Recombinant materials, in general, are an attractive biomolecule synthesis route because of the control in the specific molecular sequence, monodispersity, and ability to scale to large quantities. 100 One example is elastin-like recombinamers (ELRs), which are defined recombinant protein-based polymers (rPBPs) derived from amino acid sequences found in the hydrophobic domains of tropoelastin, the precursor to elastin which is the structural biomolecule responsible for tissue elasticity. 101 These hydrophobic amino acid domains from tropoelastin are most frequently repeats of the pentamer (VPGXG) n , where X is any amino acid except proline.…”