Nano and Micro-Structures of Elastin-Like Polypeptide-Based Materials and Their Applications: Recent Developments

Abstract

Elastin-like polypeptide (ELP) containing materials have spurred signi¯cant research interest for biomedical applications exploiting their biocompatible, biodegradable and nonimmunogenic nature while maintaining precise control over their chemical structure and functionality through genetic engineering. Physical, mechanical and biological properties of ELPs could be further manipulated using genetic engineering or through conjugation with a variety of chemical moieties. These chemical and physical modi¯cations also achieve interesting micro-and nanostructured ELPbased materials. Here, we review the recent developments during the past decade in the methods to engineer elastin-like materials, available genetic and chemical modi¯cation methods and applications of ELP micro and nanostructures in tissue engineering and drug delivery.

Synthesis and Characterization of an Array of Elastin-like Polypeptide–Polyelectrolyte Conjugates with Varying Chemistries and Amine Content for Biomedical Applications

“…5−9 ELPs are mechanically and chemically similar to extracellular matrix material, readily modifiable, and relatively straightforward to produce. 4 The biodegradability and biocompatibility of ELPs combined with their inverse phase transition behavior makes them an attractive material for in vivo and in vitro biomedical applications such as protein purification, 8,9 drug delivery, 10−15 and tissue engineering. 16−20 The hydrophobicity and T t of ELPs can be tailored to a particular application by genetically manipulating the identity of the "guest" residue X of ELP's pentapeptide sequence.…”

“…Elastin-like polypeptides (ELPs) are a family of polypeptides derived from a portion of the primary sequence of mammalian elastin, VPGXG, where V = valine, P = proline, G = glycine, and X = any amino acid except proline. − ELPs exhibit thermally induced phase transition, solubility below and coacervation above a characteristic inverse volume phase transition temperature ( T t ), and retain this property upon genetic fusion or chemical conjugation to other peptides or synthetic functional groups. − ELPs are mechanically and chemically similar to extracellular matrix material, readily modifiable, and relatively straightforward to produce . The biodegradability and biocompatibility of ELPs combined with their inverse phase transition behavior makes them an attractive material for in vivo and in vitro biomedical applications such as protein purification, , drug delivery, − and tissue engineering. − The hydrophobicity and T t of ELPs can be tailored to a particular application by genetically manipulating the identity of the “guest” residue X of ELP’s pentapeptide sequence. − Using recursive directional ligation, the identity and frequency of this guest residue can be controlled to create amphiphilic ELPs with juxtaposed segments of pentapeptide repeats featuring either hydrophilic or hydrophobic guest residues .…”