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• W1964067888 endingPage "3741" @default.
• W1964067888 startingPage "3731" @default.
• W1964067888 abstract "The recombinant proteins [EE(A)12EETGRGDSPAAS]n (n = 5,10) were prepared as a potential scaffold material for bone repair. The construct was based on Antheraea perni silk fibroin to which cells adhere well and combined poly(alanine), the integrin binding site TGRGDSPA, and a pair of glutamic acids (E2) at both the N- and C-terminal sites to render the construct water-soluble and with the hope that it might enhance mineralization with hydroxyapatite. Initially, two peptides E2(A)nE2TGRGDSPAE2(A)nE2 (n = 6, 12) were prepared by solid state synthesis to examine the effect of size on conformation and on cell binding. The larger peptide bound osteoblasts more readily and had a higher helix content than the smaller one. Titration of the side chain COO– to COOH of the E2 and D units in the peptide was monitored by solution NMR. On the basis of these results, we produced the related recombinant His tagged protein [EE(A)12EETGRGDSPAAS]n (n = 5,10) by expression in Escherichia coli. The solution NMR spectra of the recombinant protein indicated that the poly(alanine) regions are helical, and one E2 unit is helical and the other is a random coil. A molecular dynamics simulation of the protein supports these conclusions from NMR. We showed that the recombinant protein, especially, [EE(A)12EETGRGDSPAAS]10 has some of the properties required for bone tissue engineering scaffold including insolubility, and evidence of enhanced cell binding through focal adhesions, and enhanced osteogenic expression of osteoblast-like cells bound to it, and has potential for use as a bone repair material." @default.
• W1964067888 created "2016-06-24" @default.
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• W1964067888 date "2013-09-19" @default.
• W1964067888 modified "2023-10-18" @default.
• W1964067888 title "Synthesis and Characterization of Water-Soluble Silk Peptides and Recombinant Silk Protein Containing Polyalanine, the Integrin Binding Site, and Two Glutamic Acids at Each Terminal Site as a Possible Candidate for Use in Bone Repair Materials" @default.
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• W1964067888 doi "https://doi.org/10.1021/bm401118m" @default.
• W1964067888 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24004453" @default.
• W1964067888 hasPublicationYear "2013" @default.
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