Three-dimensional scaffold made from recombinant spider silk protein for tissue engineering

2009 ◽  
Vol 426 (1) ◽  
pp. 127-130 ◽  
Author(s):  
I. I. Agapov ◽  
O. L. Pustovalova ◽  
M. M. Moisenovich ◽  
V. G. Bogush ◽  
O. S. Sokolova ◽  
...  
2017 ◽  
Vol 27 (36) ◽  
pp. 1701427 ◽  
Author(s):  
Jana Petzold ◽  
Tamara B. Aigner ◽  
Filip Touska ◽  
Katharina Zimmermann ◽  
Thomas Scheibel ◽  
...  

2010 ◽  
Vol 152-153 ◽  
pp. 1734-1744 ◽  
Author(s):  
Hong Xin Wang ◽  
Zheng Xiang Xue ◽  
Mei Hong Wei ◽  
Deng Long Chen ◽  
Min Li

As a new biomaterial, recombinant spider silk protein has attracted much attention in tissue engineering. The pNSR-16/ BL21(DE3)pLysS strains fermented and produced the recombinant spider silk protein, which was then cast into scaffolds. NIH-3T3 cells were cultivated with extractions of the scaffolds in vitro. The cytotoxicity of scaffolds was analyzed with a MTT assay. The performances of cells adhesion, growth and expression on the scaffolds were observed with SEM, HE staining and immunohistochemistry. Compared with the control, the extract fluid of materials culturing the NIH-3T3 cells was not apparently different. NIH-3T3 cells could adhere and grow on the scaffolds and secret FGF-2. The pNSR-16 recombinant spider silk protein scaffolds has satisfactory cytocompatibility and the scaffolds are ideal scaffold material for tissue engineering.


2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Johannes P. M. Kramer ◽  
Tamara B. Aigner ◽  
Jana Petzold ◽  
Kaveh Roshanbinfar ◽  
Thomas Scheibel ◽  
...  

2020 ◽  
Vol 8 (9) ◽  
pp. 2514-2525
Author(s):  
Carolina Åstrand ◽  
Veronique Chotteau ◽  
Anna Falk ◽  
My Hedhammar

The functionalized recombinant spider silk protein FN-silk can self-assemble into a 3D microfiber network. When combined with recombinant laminin521 it provides a 3D culture system suitable for expansion of hPSCs and following neural differentiation.


Materials ◽  
2016 ◽  
Vol 9 (7) ◽  
pp. 560 ◽  
Author(s):  
John Hardy ◽  
Jose Torres-Rendon ◽  
Aldo Leal-Egaña ◽  
Andreas Walther ◽  
Helmut Schlaad ◽  
...  

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 511
Author(s):  
Yu Suzuki ◽  
Takanori Higashi ◽  
Takahiro Yamamoto ◽  
Hideyasu Okamura ◽  
Takehiro K. Sato ◽  
...  

Spider dragline silk is a biopolymer with excellent mechanical properties. The development of recombinant spider silk protein (RSP)-based materials with these properties is desirable. Formic acid (FA) is a spinning solvent for regenerated Bombyx mori silk fiber with excellent mechanical properties. To use FA as a spinning solvent for RSP with the sequence of major ampullate spider silk protein from Araneus diadematus, we determined the conformation of RSP in FA using solution NMR to determine the role of FA as a spinning solvent. We assigned 1H, 13C, and 15N chemical shifts to 32-residue repetitive sequences, including polyAla and Gly-rich regions of RSP. Chemical shift evaluation revealed that RSP is in mainly random coil conformation with partially type II β-turn structure in the Gly-Pro-Gly-X motifs of the Gly-rich region in FA, which was confirmed by the 15N NOE data. In addition, formylation at the Ser OH groups occurred in FA. Furthermore, we evaluated the conformation of the as-cast film of RSP dissolved in FA using solid-state NMR and found that β-sheet structure was predominantly formed.


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