Recombination and Purification of Elastin-Like Polypeptides.

Abstract

Elastin, as an extracellular matrix protein, has inherent advantages for biomedical applications. For example, it is highly extensible and biocompatible, biodegradable, and has no immunogenicity. However, directly extracting elastin from biological tissues remains challenging because they usually coexist with other proteins such as collagen. Therefore, an effective strategy to produce elastin is to transfer the elastin's target gene into other expression hosts and synthesize the resultant polypeptides using chemical biology methods. The polypeptides and proteins produced using these methods are usually referred to as elastin-like peptides (ELPs), which have received intensive interests in drug delivery and release, tissue engineering, implanted devices, and so on. Therefore, this chapter introduces the detailed protocol for the preparation of ELPs using genetic recombination, including DNA recombination, expression, and purification. The methods presented here are expected to provide methodological guidance for preparation and application of ELP materials.