Photoresponsive Retinal-Modified Silk–Elastin Copolymer

Sun, Zhongyuan; Qin, Guokui; Xia, Xiao-Xia; Cronin‐Golomb, Mark; Omenetto, Fiorenzo G.; Kaplan, David L.

doi:10.1021/ja312647n

Cited by 21 publications

(22 citation statements)

References 28 publications

(65 reference statements)

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“…[23] To date, characterization of SELP films remains largely unknown and only a few studies report their use. [17,[24][25][26] SELP films showed to be optically transparent to visible light, with mechanical properties in hydrated conditions comparable to those of native soft tissues. [17,26] Moreover, the good optical properties of SELP-47K films, together with its high in vitro cytocompatibility and ability to encapsulate and release drugs, suggested that these may be attractive material candidates for ophthalmic devices.…”

Section: Introductionmentioning

confidence: 92%

“…A traditional approach to improve the flexibility of given materials is by blending polymers with suitable plasticizers and in fact previous studies have shown that improved elongation at break could be obtained by adding glycerol to the polymer solution prior to solvent casting . To date, characterization of SELP films remains largely unknown and only a few studies report their use . SELP films showed to be optically transparent to visible light, with mechanical properties in hydrated conditions comparable to those of native soft tissues .…”

Section: Introductionmentioning

confidence: 99%

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Exploring the Properties of Genetically Engineered Silk‐Elastin‐Like Protein Films

Machado

Costa

Sencadas

et al. 2015

Macromolecular Bioscience

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Free standing films of a genetically engineered silk-elastin-like protein (SELP) were prepared using water and formic acid as solvents. Exposure to methanol-saturated air promoted the formation of aggregated β-strands rendering aqueous insolubility and improved the mechanical properties leading to a 10-fold increase in strain-to-failure. The films were optically clear with resistivity values similar to natural rubber and thermally stable up to 180 °C. Addition of glycerol showed to enhance the flexibility of SELP/glycerol films by interacting with SELP molecules through hydrogen bonding, interpenetrating between the polymer chains and granting more conformational freedom. This detailed characterization provides cues for future and unique applications using SELP based biopolymers.

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Section: Introductionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Exploring the Properties of Genetically Engineered Silk‐Elastin‐Like Protein Films

Machado

Costa

Sencadas

et al. 2015

Macromolecular Bioscience

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“…Biologically inspired peptide‐based materials are of increasing interest for applications where biological function and structure are used outside of the natural context . Among them, a specific class of repetitive polypeptides termed elastin‐like polypeptides (ELPs) have been extensively studied for various medical applications such as tissue engineering, diagnostics, biolubrication, and drug delivery . Until now, ELPs have been investigated almost exclusively in aqueous environments or in the crosslinked hydrogel state.…”

Section: Summary Of the Mesomorphisms Of Gfp–sups (Gfp–e9 Gfp–e18 Gmentioning

confidence: 99%

Solvent‐Free Liquid Crystals and Liquids Based on Genetically Engineered Supercharged Polypeptides with High Elasticity

Liu

Pesce

et al. 2015

Advanced Materials

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or traditional organic liquid crystals. Therefore, the development of a general strategy for fabricating solvent-free ELP fl uids (liquid crystals and liquids) is an attractive goal.Genetic engineering as a recombinant protein synthesis technology affords a powerful tool for the synthesis of ELPs with predictable properties and biofunctionality. Engineered ELPs allow fabrication of desired sequences with high molecular weights combined with monodispersity, well-defi ned structures and chain lengths that are impossible to be achieved by chemical synthesis. [31][32][33] We demonstrate here the creation of genetically engineered ELPs based on the common pentameric repeat sequence (VPG X G) n found in tropoelastin by taking advantage of the fl exibility of the amino acid composition at the fourth position of that peptide motif. First, glutamic acid was introduced at this site of the repeat to transform the ELPs into supercharged polypeptides (SUPs, (VPG E G) n ). Then, green fl uorescent protein (GFP) was fused to the SUP for an additional level of functionality. Thus, a series of GFP-SUPs (GFP-(VPG E G) n ) with negative charges ranging from 9, over 18, 36, 72 to 144 (GFP-E9, GFP-E18, GFP-E36, GFP-E72, and GFP-E144) were expressed in E. coli (details in Figure S1-S3, Supporting Information). The purity and molecular weights of the products were confi rmed by polyacrylamide gel electrophoresis and matrix-assisted laser desorption/ionization time-of-fl ight mass spectrometry, respectively ( Figure S4 and S5, Supporting Information). Subsequently, the GFP-SUPs were complexed with cationic surfactants. This was inspired by previous work dealing with polyelectrolyte-surfactant complexation via electrostatic interactions. [34][35][36][37][38] In the context of proteins, complexation between cationized ferritin and anionic polymer surfactants yielded mesophases with a narrow temperature range. [ 37 ] Here we propose that the combination of negatively charged GFP-SUP with positively charged surfactants, followed by dehydration, can act as a simple generic scheme for producing solventfree GFP-SUP fl uids. In the present experiments, electrostatic interactions as the driving force couple these GFP-SUPs and surfactants into hybrid lamellar assemblies ( Figure 1 ), where the fl exible alkyl chains of surfactants suppress crystallization. [ 34,35 ] The anhydrous SUP-surfactant complexes exhibit non-Newtonian (smectic liquid crystal) and Newtonian (isotropic liquid) fl uid behaviors. The lengths of the SUP and surfactant are found to be extremely important in tuning the physical properties of the fl uids. We fi nd a high elasticity in the SUP mesophases when they are ordered in smectic layers. The elastic moduli of these phases are larger than the ones reported Biologically inspired peptide-based materials are of increasing interest for applications where biological function and structure are used outside of the natural context. [1][2][3][4][5][6][7][8][9][10] Among them, a specifi c class of repetitive polypeptides termed elasti...

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“…In addition, a recombinant SELP named PS2E8K was synthesized and chemically modified via the lysine residues present in the elastin block as guest residue with the biocompatible moiety retinal protonated Schiff base (RPSB) to generate a material for light‐induced dynamic changes. Birefringence was induced when the recombinamer was irradiated with linearly polarized 488 nm laser light, thereby suggesting its application in eye tissue engineering …”

Section: Recombinant Silk Proteinsmentioning

confidence: 98%

Recombinant Technology in the Development of Materials and Systems for Soft‐Tissue Repair

Girotti

Orbanić

Ibáñez‐Fonseca

et al. 2015

Adv Healthcare Materials

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The field of biomedicine is constantly investing significant research efforts in order to gain a more in-depth understanding of the mechanisms that govern the function of body compartments and to develop creative solutions for the repair and regeneration of damaged tissues.The main overall goal is to develop relatively simple systems that are able to mimic naturally occurring constructs and can therefore be used in regenerative medicine.Recombinant technology, which is widely used to obtain new tailored synthetic genes that express polymeric protein-based structures, now offers a broad range of advantages for that purpose by permitting the tuning of biological and mechanical properties depending on the 2 intended application while simultaneously ensuring adequate biocompatibility and biodegradability of the scaffold formed by the polymers. This review is focused on recombinant protein-based materials that resemble naturally occurring proteins of interest for use in soft tissue repair. An overview of recombinant biomaterials derived from elastin, silk, collagen and resilin will be given, along with a description of their characteristics and suggested applications. Current endeavors in this field are continuously providing moreimproved materials in comparison with conventional ones. As such, a great effort is being made to put these materials through clinical trials in order to favor their future use.

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Photoresponsive Retinal-Modified Silk–Elastin Copolymer

Cited by 21 publications

References 28 publications

Exploring the Properties of Genetically Engineered Silk‐Elastin‐Like Protein Films

Exploring the Properties of Genetically Engineered Silk‐Elastin‐Like Protein Films

Solvent‐Free Liquid Crystals and Liquids Based on Genetically Engineered Supercharged Polypeptides with High Elasticity

Recombinant Technology in the Development of Materials and Systems for Soft‐Tissue Repair

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