Elastic Protein-Based Biomaterials

Urry, Dan W.; Woods, Copper; Hayes, Larry; Xu, Jie; McPherson, David T.; Parker, Timothy M.; Iwama, Masamichi; Furutan, Masakazu; Hayashi, Toshio; Murata, Mitsuhiro

doi:10.1201/9780203913338.ch2

Cited by 5 publications

(1 citation statement)

References 30 publications

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“…First-Generation Polypeptide Libraries. Our initial experiments with the adaptive DNA methods reproduced literature precedent 15d,e in construction and expression of both 22 (A2-8F13, Figure a, X 1 =X 2 =X=X=F) and the slightly and asymmetrically modified 23 (A2-16YF12, Figure a, X 1 =X 3 =Y, X 2 =X 4 =F). It was determined that the hydrophobicity of these peptides imparted a profound tendency to aggregate.…”

Section: Resultssupporting

confidence: 56%

Design and Preparation of β-Sheet Forming Repetitive and Block-Copolymerized Polypeptides

et al. 2007

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The design and rapid construction of libraries of genes coding beta-sheet forming repetitive and block-copolymerized polypeptides bearing various C- and N-terminal sequences are described. The design was based on the assembly of DNA cassettes coding for the (GA)3GX amino acid sequence where the (GAGAGA) sequences would constitute the beta-strand units of a larger beta-sheet assembly. The edges of this beta-sheet would be functionalized by the turn-inducing amino acids (GX). The polypeptides were expressed in Escherichia coli using conventional vectors and were purified by Ni-nitriloacetic acid (NTA) chromatography. The correlation of polymer structure with molecular weight was investigated by gel electrophoresis and mass spectrometry. The monomer sequences and post-translational chemical modifications were found to influence the mobility of the polypeptides over the full range of polypeptide molecular weights while the electrophoretic mobility of lower molecular weight polypeptides was more susceptible to C- and N-termini polypeptide modifications.

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Section: Resultssupporting

confidence: 56%

Design and Preparation of β-Sheet Forming Repetitive and Block-Copolymerized Polypeptides

et al. 2007

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Hybrid Nanotopographical Surfaces Obtained by Biomimetic Mineralization of Statherin‐Inspired Elastin‐Like Recombinamers

Chen

Ribeiro

et al. 2014

Adv Healthcare Materials

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Modification of surfaces mimicking unique chemical and physical features of mineralized tissues is of major interest for obtaining biomaterials for replacing and regenerating biological tissues. Here, human salivary statherin-inspired genetically engineered recombinamers (ELRs, HSS) on biomedical surfaces regulates mineralization to form an amorphous-calcium-phosphate (ACP) layer that reproduces the original substrate nanotopography. The HSS-ELRs carry a statherin-derived peptide with high affinity to tooth enamel. They are tethered to nanorough surfaces and mineralized using an enzyme-directed process. A homogeneous layer of ACP-minerals forms on HSS-coated surfaces retaining the original nanotopography of the substrate. In contrast, biomineralization of control surfaces results in uncontrolled growth of minerals. This suggest the statherin-inspired ELRs have ability to induce and control growth of the minerals on the biofunctional surfaces. Likely, the HSS-ELR coating have similar bioactivity to that of statherin in human saliva. The hybrid nanorough surfaces improve adhesion and differentiation of preosteoblasts and show potential for dental and orthopedic implants integration. This method enables the combination and tailoring of nanotopographical and biochemical cues to design functionalized surfaces to investigate and potentially direct the stem cell fate.

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Advanced Materials for the Future: Protein-based Materials with Potential to Sustain Individual Health and Societal Development

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Elastic Protein-Based Biomaterials

Cited by 5 publications

References 30 publications

Design and Preparation of β-Sheet Forming Repetitive and Block-Copolymerized Polypeptides

Design and Preparation of β-Sheet Forming Repetitive and Block-Copolymerized Polypeptides

Hybrid Nanotopographical Surfaces Obtained by Biomimetic Mineralization of Statherin‐Inspired Elastin‐Like Recombinamers

Advanced Materials for the Future: Protein-based Materials with Potential to Sustain Individual Health and Societal Development

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