Abstract
Elastin-like polypeptides (ELP) are artificial, genetically encodable biopolymers, belonging to elastomeric proteins, which are widespread in a wide range of living organisms. They are composed of a repeating pentapeptide sequence Val–Pro–Gly–Xaa–Gly, where the guest residue (Xaa) can be any naturally occurring amino acid except proline. These polymers undergo reversible phase transition that can be triggered by various environmental stimuli, such as temperature, pH or ionic strength. This behavior depends greatly on the molecular weight, concentration of ELP in the solution and composition of the amino acids constituting ELPs. At a temperature below the inverse transition temperature (Tt), ELPs are soluble, but insoluble when the temperature exceeds Tt. Furthermore, this feature is retained even when ELP is fused to the protein of interest. These unique properties make ELP very useful for a wide variety of biomedical applications (e.g. protein purification, drug delivery etc.) and it can be expected that smart biopolymers will play a significant role in the development of most new materials and technologies. Here we present the structure and properties of thermally responsive elastin-like polypeptides with a particular emphasis on biomedical and biotechnological application.
Highlights
At present, owing to the improvement in our understanding of the structure of proteins and availability of advanced tools in molecular biology, genetic and protein engineering, synthesizing DNA fragments encoding any amino acid sequences of proteins is possible with practically no restrictions (Tchoudakova et al 2009; Chen et al 2010)
Recursive directional ligation rivals other strategies for assembling synthetic genes encoding proteins with a repetitive structure because: (1) a polymer with the molecular mass needed for the applications in question is produced, (2) each recursive directional ligation (RDL) round generates identical DNA oligomers, eliminating the necessity of their multiple sequencing, (3) a library of potentially useful, smaller genes is created in the process of assembling large genes, (4) monomers or oligomers encoding different peptides or proteins can be freely joined in every repeat of the reaction, which allows the structural diversity of the polymer to be increased (McDaniel et al 2010b)
This paper focuses only on elastin-like polypeptides containing repeats of the Elastin-like polypeptides (ELP)[VPGXG-n] pentapeptide, which are most often described in the literature
Summary
At present, owing to the improvement in our understanding of the structure of proteins and availability of advanced tools in molecular biology, genetic and protein engineering, synthesizing DNA fragments encoding any amino acid sequences of proteins is possible with practically no restrictions (Tchoudakova et al 2009; Chen et al 2010). Encoding the polymer sequence at the gene level allows control over the composition of polymer subunits that is hard to achieve through chemical polymerization. Molecules synthesized in this way may show many properties important for their use, such as biocompatibility, biodegradability or reacting to changes in the ambient conditions in a certain way. Inverse temperature transition (ITT) makes them part and parcel of the rapidly developing new technologies in the field of tissue (Amruthwar and Janorkar 2013; Machado et al 2013), protein, and material engineering or the techniques for the purification of recombinant proteins (Kwon and Cho 2012; Duvenage et al 2013). We discuss current application of ELP in therapeutic peptide and drug delivery, tissue engineering, recombinant protein purification or removal of heavy metals
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