Elastomeric recombinant protein-based biomaterials

Annabi, Nasim; Mithieux, Suzanne M.; Camci‐Unal, Gulden; Dokmeci, Mehmet R.; Weiss, Anthony S.; Khademhosseini, Ali

doi:10.1016/j.bej.2013.05.006

Cited by 92 publications

(69 citation statements)

References 108 publications

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“…The resulting advantages, such as the straightforward design of the monomers and almost complete monodispersity, have attracted the interest of the scientists seeking novel designer polymeric materials. Examples of proteinaceous materials studied for biochemical and industrial applications include elastins [1,2], collagens [3], silks [4], keratins [5], and mussel proteins [6]. In general, the properties of these proteins are dictated by ordered secondary structures that promote self-assembly of the molecules.…”

Section: Introductionmentioning

confidence: 99%

Engineering thermal properties of elastin-like polypeptides by incorporation of unnatural amino acids in a cell-free protein synthesis system

Catherine

Lee

et al. 2015

Biotechnol Bioproc E

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Based on the central dogma of protein synthesis, traditional methods for protein engineering require that altering protein structure and function must be accompanied by changing the nucleotide sequence of the genes encoding the protein. However, the preparation of a template gene for each individual protein requires a great deal of time and effort, thereby limiting the throughput and scope of studying engineered proteins. In this study, we describe translation-level engineering of proteins using cell-free protein synthesis. Taking advantage of the promiscuity of aminoacyl tRNA synthetases in accepting structurally similar amino acid analogues, unnatural amino acids were introduced into elastin-like polypeptides in place of the corresponding cognate amino acids. Through the incorporation of various analogues and starting from the same gene, the phase transition temperatures of elastin-like polypeptides became tunable. Our results demonstrate the usefulness of cell-free protein synthesis for protein engineering using unnatural amino acids without the need for cloning.

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Section: Introductionmentioning

confidence: 99%

Engineering thermal properties of elastin-like polypeptides by incorporation of unnatural amino acids in a cell-free protein synthesis system

Catherine

Lee

et al. 2015

Biotechnol Bioproc E

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“…These coacervated tropoelastin molecules then align with each other. Covalent crosslinking of hydrophilic domains, particularly those rich in Lys and Ala ensues resulting in the formation of a stabilized mature elastic protein polymer network [6,8,10]. The rubber-like properties of elastin are due to repetitive modules such as VPGXG[3,11].…”

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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“…Several excellent reviews related to ELP-based biomaterials and their applications have appeared in the literature over the past decade. [2][3][4][5][6][7][8][9][10][11] This review should not be treated as exhaustive, but one that focuses on the various examples of research related to the rational design and development of ELP-based biomaterials that include engineering elastin-like materials, their modi¯cation through genetic and chemical means and their applications in the¯elds of tissue engineering and drug delivery. We have primarily included research published during the last decade with a particular attention to the unique and remarkable aspects of nano and microstructures of the ELPs when summarizing these aspects.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2013

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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.

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Elastomeric recombinant protein-based biomaterials

Cited by 92 publications

References 108 publications

Engineering thermal properties of elastin-like polypeptides by incorporation of unnatural amino acids in a cell-free protein synthesis system

Engineering thermal properties of elastin-like polypeptides by incorporation of unnatural amino acids in a cell-free protein synthesis system

Elastic proteins and elastomeric protein alloys

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

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