Amphiphilic Elastin-Like Block Co-Recombinamers Containing Leucine Zippers: Cooperative Interplay between Both Domains Results in Injectable and Stable Hydrogels

Fernández‐Colino, Alicia; Arias, Francisco J.; Alonso, Matilde; Rodríguez-Cabello, J Carlos

doi:10.1021/acs.biomac.5b01103

Cited by 36 publications

(37 citation statements)

References 26 publications

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“…[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]. The later refers to a phase transition from soluble to insoluble that the ELR experiences in response to an environmental stimulus (e.g.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Macroporous click-elastin-like hydrogels for tissue engineering applications

Fernández‐Colino

Wolf

Keijdener

et al. 2018

Materials Science and Engineering: C

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Elastin is a key extracellular matrix (ECM) protein that imparts functional elasticity to tissues and therefore an attractive candidate for bioengineering materials. Genetically engineered elastin-like recombinamers (ELRs) maintain inherent properties of the natural elastin (e.g. elastic behavior, bioactivity, low thrombogenicity, inverse temperature transition) while featuring precisely controlled composition, the possibility for biofunctionalization and non-animal origin. Recently the chemical modification of ELRs to enable their crosslinking via a catalyst-free click chemistry reaction, has further widened their applicability for tissue engineering. Despite these outstanding properties, the generation of macroporous click-ELR scaffolds with controlled, interconnected porosity has remained elusive so far. This significantly limits the potential of these materials as the porosity has a crucial role on cell infiltration, proliferation and ECM formation. In this study we propose a strategy to overcome this issue by adapting the salt leaching/gas foaming technique to click-ELRs. As result, macroporous hydrogels with tuned pore size and mechanical properties in the range of many native tissues were reproducibly obtained as demonstrated by rheological measurements and quantitative analysis of fluorescence, scanning electron and two-photon microscopy images. Additionally, the appropriate size and interconnectivity of the pores enabled smooth muscle cells to migrate into the click-ELR scaffolds and deposit extracellular matrix. The macroporous structure together with the elastic performance and bioactive character of ELRs, the specificity and non-toxic character of the catalyst-free click-chemistry reaction, make these scaffolds promising candidates for applications in tissue regeneration. This work expands the potential use of ELRs and click chemistry systems in general in different biomedical fields.

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Section: Accepted Manuscriptmentioning

confidence: 99%

Macroporous click-elastin-like hydrogels for tissue engineering applications

Fernández‐Colino

Wolf

Keijdener

et al. 2018

Materials Science and Engineering: C

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“…Fernandez-Colino et al created ELPs with paired leucine zippers at the N-and C-termini. [153] Above the T t of the ELP, the synergistic effect of hydrophobic interactions of ELP and the dimerization domains resulted in the formation of an interconnected microporous network that could be used as a cell culture scaffold. Park and Champion used a single terminal leucine zipper to noncova-lently bind globular fluorescent proteins to ELPs ( Figure 6).…”

Section: Alpha Helicesmentioning

confidence: 99%

Engineering the Architecture of Elastin‐Like Polypeptides: From Unimers to Hierarchical Self‐Assembly

Saha

Banskota

Roberts

et al. 2020

Advanced Therapeutics

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Well‐defined tunable nanostructures formed through the hierarchical self‐assembly of peptide building blocks have drawn significant attention due to their potential applications in biomedical science. Artificial protein polymers derived from elastin‐like polypeptides (ELPs), which are based on the repeating sequence of tropoelastin (the water‐soluble precursor to elastin), provide a promising platform for creating nanostructures due to their biocompatibility, ease of synthesis, and customizable architecture. By designing the sequence and composition of ELPs at the gene level, their physicochemical properties can be controlled to a degree that is unmatched by synthetic polymers. A variety of ELP‐based nanostructures are designed, inspired by the self‐assembly of elastin and other proteins in biological systems. The choice of building blocks determines not only the physical properties of the nanostructures, but also their self‐assembly into architectures ranging from spherical micelles to elongated nanofibers. This review focuses on the molecular determinants of ELP and ELP‐hybrid self‐assembly and formation of spherical, rod‐like, worm‐like, fibrillar, and vesicle architectures. A brief discussion of the potential biomedical applications of these supramolecular assemblies is also included.

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“…Covalent bonds can also be introduced within the self‐assembly domains. In a work conducted by Fernández‐Colino et al, a leucine zipper sequence with intrinsic cysteine residues was utilized to make self‐assembled hydrogels . Leucine zippers were fused on two ends of an ELP domain (EI‐ZC) with an LCST at 16 °C.…”

Section: Self‐assemblymentioning

confidence: 99%

Designing Smart Materials with Recombinant Proteins

Hollingshead

Lin

Liu

2017

Macromolecular Bioscience

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Recombinant protein design allows modular protein domains with different functionalities and responsive behaviors to be easily combined. Inclusion of these protein domains can enable recombinant proteins to have complex responses to their environment (e.g., temperature-triggered aggregation followed by enzyme-mediated cleavage for drug delivery or pH-triggered conformational change and self-assembly leading to structural stabilization by adjacent complementary residues). These “smart” behaviors can be tuned by amino acid identity and sequence, chemical modifications, and addition of other components. A wide variety of domains and peptides have smart behavior. In this review, we will focus on protein designs for self-assembly or conformational changes due to stimuli such as shifts in temperature or pH.

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Amphiphilic Elastin-Like Block Co-Recombinamers Containing Leucine Zippers: Cooperative Interplay between Both Domains Results in Injectable and Stable Hydrogels

Cited by 36 publications

References 26 publications

Macroporous click-elastin-like hydrogels for tissue engineering applications

Macroporous click-elastin-like hydrogels for tissue engineering applications

Engineering the Architecture of Elastin‐Like Polypeptides: From Unimers to Hierarchical Self‐Assembly

Designing Smart Materials with Recombinant Proteins

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