Fabricated Elastin

Yeo, Giselle C.; Aghaei-Ghareh-Bolagh, Behnaz; Brackenreg, Edwin P.; Hiob, Matti A.; Lee, Pearl; Weiss, Anthony S.

doi:10.1002/adhm.201400781

Cited by 103 publications

(99 citation statements)

References 317 publications

(491 reference statements)

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“…In the latter system, LLPS of monomeric elastin results in hydrated protein-rich coacervate droplets that are deposited and crosslinked to form an elastic matrix (7,8). In addition to their fundamental importance to biology, the dynamic reversibility of LLPS makes phase-separated states of proteins an attractive platform for development of responsive biomaterials with broad application, for instance as scaffolds for tissue engineering or as carriers in drug delivery systems (9)(10)(11).…”

mentioning

confidence: 99%

Direct observation of structure and dynamics during phase separation of an elastomeric protein

Reichheld

Muiznieks

Keeley

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

225

245

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Despite its growing importance in biology and in biomaterials development, liquid-liquid phase separation of proteins remains poorly understood. In particular, the molecular mechanisms underlying simple coacervation of proteins, such as the extracellular matrix protein elastin, have not been reported. Coacervation of the elastin monomer, tropoelastin, in response to heat and salt is a critical step in the assembly of elastic fibers in vivo, preceding chemical crosslinking. Elastin-like polypeptides (ELPs) derived from the tropoelastin sequence have been shown to undergo a similar phase separation, allowing formation of biomaterials that closely mimic the material properties of native elastin. We have used NMR spectroscopy to obtain site-specific structure and dynamics of a self-assembling elastin-like polypeptide along its entire self-assembly pathway, from monomer through coacervation and into a cross-linked elastic material. Our data reveal that elastin-like hydrophobic domains are composed of transient β-turns in a highly dynamic and disordered chain, and that this disorder is retained both after phase separation and in elastic materials. Cross-linking domains are also highly disordered in monomeric and coacervated ELP 3 and form stable helices only after chemical cross-linking. Detailed structural analysis combined with dynamic measurements from NMR relaxation and diffusion data provides direct evidence for an entropy-driven mechanism of simple coacervation of a protein in which transient and nonspecific intermolecular hydrophobic contacts are formed by disordered chains, whereas bulk water and salt are excluded.phase separation | elastin | NMR | protein structure | dynamics T he liquid-liquid phase separation (LLPS) of molecules has long been exploited to concentrate and encapsulate molecules for drug delivery and food preparation (1, 2). In biology, there is increasing awareness that many proteins exhibit this type of phase behavior, allowing transient microenvironments to be quickly assembled and disassembled in response to changing solution conditions, or the availability of binding partners (3, 4). Protein phase separation occurs intracellularly to generate various membraneless organelles, such as ribonucleoprotein (RNP) bodies involved in nucleic acid processing, transport, and storage (5). A similar phenomenon is observed in the extracellular matrix as a critical step in the synthesis of elastic fibers, which provide extensibility, recoil, and resilience to tissues (6, 7). In the latter system, LLPS of monomeric elastin results in hydrated protein-rich coacervate droplets that are deposited and crosslinked to form an elastic matrix (7,8). In addition to their fundamental importance to biology, the dynamic reversibility of LLPS makes phase-separated states of proteins an attractive platform for development of responsive biomaterials with broad application, for instance as scaffolds for tissue engineering or as carriers in drug delivery systems (9-11).Despite the keen interest in proteins that undergo s...

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mentioning

confidence: 99%

Direct observation of structure and dynamics during phase separation of an elastomeric protein

Reichheld

Muiznieks

Keeley

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

225

245

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“…They have been recently reviewed in-depth 88 , therefore, this section will briefly describe the sources of elastin available and the current technologies available for creating biomaterials.…”

Section: Elastin and Tropoelastin: Role In Tissue Repair And Maintmentioning

confidence: 99%

Elastin-based biomaterials and mesenchymal stem cells

et al. 2015

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Elastin is the dominant mammalian elastic protein found in soft tissue. Elastin-based biomaterials have the potential to repair elastic tissues by improving local elasticity and providing appropriate cellular interactions and signaling. Studies that combine these biomaterials with mesenchymal stem cells have demonstrated their capacity to also regenerate non-elastic tissue. Mesenchymal stem cell differentiation can be controlled by their immediate environment, and their sensitivity to elasticity makes them an ideal candidate for combining with elastin-based biomaterials. With the growing accessibility of the elastin precursor, tropoelastin, and elastin-derived materials, the amount of research interest in combining these two fields has increased and, subsequently, is leading to the realization of a potentially new strategy for regenerative medicine.

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“…Tropoelastin-based hydrogels can be prepared by chemical crosslinking using bis-sulfosuccinimidyl suberate (BS3) and glutaraldehyde [18,25,26] that benefit from the availability of 35 juxtaposed lysine residues across the molecule. Physical crosslinking has been used to produce elastic hydrogels.…”

Section: Introductionmentioning

confidence: 99%

“…In order to improve their mechanical properties, these proteins have been used in combination with other natural or synthetic polymers to produce materials with a range of different mechanical, physical and biological properties to match different tissues types. Blended tropoelastin materials have been reviewed recently [26]. Here we focus on tropoelastin/silk- and resilin/silk- based hybrid materials.…”

Section: Introductionmentioning

confidence: 99%

Elastic proteins and elastomeric protein alloys

Aghaei-Ghareh-Bolagh

Mithieux

Weiss

2016

Current Opinion in Biotechnology

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The elastomeric proteins elastin and resilin have been used extensively in the fabrication of biomaterials for tissue engineering applications due to their unique mechanical and biological properties. Tropoelastin is the soluble monomer component of elastin. Tropoelastin and resilin are both highly elastic with high resilience, substantial extensibility, high durability and low energy loss, which makes them excellent candidates for the fabrication of elastic tissues that demand regular and repetitive movement like the skin, lung, blood vessels, muscles and vocal folds. Combinations of these proteins with silk fibroin further enhance their biomechanical and biological properties leading to a new class of protein alloy materials with versatile properties. In this review, the properties of tropoelastin- and resilin-based biomaterials with and without silk are described in concert with examples of their applications in tissue engineering.

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Fabricated Elastin

Cited by 103 publications

References 317 publications

Direct observation of structure and dynamics during phase separation of an elastomeric protein

Direct observation of structure and dynamics during phase separation of an elastomeric protein

Elastin-based biomaterials and mesenchymal stem cells

Elastic proteins and elastomeric protein alloys

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