Recent Contributions of Elastin-Like Recombinamers to Biomedicine and Nanotechnology

Abstract

Abstract:The emergence of the new scientific field known as nanomedicine is being catalyzed by multiple improvements in nanoscience techniques and significant progress in materials science, especially as regards the testing of novel and sophisticated biomaterials. This conjuncture has furthered the development of promising instruments in terms of detection, bioanalysis, therapy, diagnostics and imaging. Some of the most innovative new biomaterials are protein-inspired biomimetic materials in which modern biotechnology and genetic-engineering techniques complement the huge amount of information afforded by natural protein evolution to create advanced and tailor-made multifunctional molecules. Amongst these protein-based biomaterials, Elastin-like Recombinamers (ELRs) have demonstrated their enormous potential in the fields of biomedicine and nanoscience in the last few years. This broad applicability derives from their unmatched properties, particularly their recombinant and tailor-made nature, the intrinsic characteristics derived from their elastin-based origin (mainly their mechanical properties and ability to self-assemble as a result of their stimuli-responsive behavior), their proven biocompatibility and biodegradability, as well as their versatility as regards incorporating advanced chemical or recombinant modifications into the original structure that open up an almost unlimited number of multifunctional possibilities in this developing field. This article provides an updated review of the recent challenges overcome by using these recombinant biomaterials in the fields of nano-and biomedicine, ranging from nanoscale applications in surface modifications and self-assembled nanostructures to drug delivery and regenerative medicine.

Macroporous click-elastin-like hydrogels for tissue engineering applications

“…They are produced by genetic engineering techniques, [4] which ensures an absolute control over the amino acid composition and the achievement of a completely monodisperse material. [5] Furthermore, functional groups can be inserted in the repeating sequence obtaining in this way desired bioactive properties. ELRs have been shown to maintain important aspects of the natural elastin, such as the elastic behavior, the cytocompatibility, [6,7] the low thrombogenicity [8][9][10] and the inverse transition behavior [11].…”

“…All these properties explain the increasing interest for these materials in biomedical applications. [5,[12][13][14] We have recently shown that ELRs could be chemically modified at their lysine groups to bear azide and cyclooctyne groups to enable the formation of hydrogels by a catalyst-free click chemistry reaction [15] . Click chemistry [16][17][18][19] (and concretely Huisgen 1,3-dipolar cycloadition of azides and alkynes) has proven itself to be superior to other crosslinking…”

Genetically Engineered Elastin-based Biomaterials for Biomedical Applications

“…Thus, they can be used as soluble delivery systems when fused to therapeutic proteins in a recombinant manner, or as pharmacokinetic enhancers, either by chemical conjugation or by fusion protein expression of the drug [17]. A monomeric ELR carrier allows the pharmacokinetics and biodistribution of its drug load to be improved when compared to the free drug, thus resulting in specific delivery of the therapeutic agent [18]. Moreover, the genetic engineering of elastin-like recombinamers allows targeting peptides, such as receptor ligands or cell-penetrating domains, to be incorporated and reactive sites useful for covalent chemical conjugation of drugs to be included into the ELR sequence [19].…”

A novel lipase-catalyzed method for preparing ELR-based bioconjugates

“…This is the case for elastin-like recombinamers (ELRs), a type of recombinant biopolymers with a structure based on elastin, the extracellular elastic protein found in higher animals [1]. As these recombinamers are designed at the gene level, the high precision control in gene construction is transferred onwards into the final polypeptide, thus meaning that their physical and bioactive properties can be finely tuned as desired using the most appropriate amino acid composition for different biomedical and nanotechnological applications [2][3][4]. The degree of control and complexity of such recombinamers is not practically achievable using more conventional synthetic technologies.…”