An Engineered Spider Silk Protein Forms Microspheres

2008 ◽  
Vol 47 (24) ◽  
pp. 4592-4594 ◽  
Author(s):  
Ute K. Slotta ◽  
Sebastian Rammensee ◽  
Stanislav Gorb ◽  
Thomas Scheibel
Keyword(s):  
Spider Silk ◽  
Silk Protein ◽  
Spider Silk Protein

scholarly journals Presence of β-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 511
Author(s):  
Yu Suzuki ◽  
Takanori Higashi ◽  
Takahiro Yamamoto ◽  
Hideyasu Okamura ◽  
Takehiro K. Sato ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Formic Acid ◽  
Spider Silk ◽  
Chemical Shifts ◽  
Repetitive Sequences ◽  
Silk Protein ◽  
Random Coil ◽  
Oh Groups ◽  
Spider Silk Protein ◽  
Turn Structure

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.

scholarly journals Interfacial Behavior of Recombinant Spider Silk Protein Parts Reveals Cues on the Silk Assembly Mechanism

Langmuir ◽  
2018 ◽  
Vol 34 (39) ◽  
pp. 11795-11805 ◽  
Author(s):  
Linnea Nilebäck ◽  
Suvi Arola ◽  
Mathias Kvick ◽  
Arja Paananen ◽  
Markus B. Linder ◽  
...  
Keyword(s):  
Spider Silk ◽  
Silk Protein ◽  
Interfacial Behavior ◽  
Assembly Mechanism ◽  
Spider Silk Protein

Glycopolymer Functionalization of Engineered Spider Silk Protein-based Materials for Improved Cell Adhesion

2014 ◽  
Vol 14 (7) ◽  
pp. 936-942 ◽  
Author(s):  
John G. Hardy ◽  
André Pfaff ◽  
Aldo Leal-Egaña ◽  
Axel H. E. Müller ◽  
Thomas R. Scheibel
Keyword(s):  
Cell Adhesion ◽  
Spider Silk ◽  
Silk Protein ◽  
Spider Silk Protein

Interactions of Fibroblasts with Different Morphologies Made of an Engineered Spider Silk Protein

2011 ◽  
Vol 14 (3) ◽  
pp. B67-B75 ◽  
Author(s):  
Aldo Leal-Egaña ◽  
Gregor Lang ◽  
Carolin Mauerer ◽  
Jasmin Wickinghoff ◽  
Michael Weber ◽  
...  
Keyword(s):  
Spider Silk ◽  
Silk Protein ◽  
Spider Silk Protein

Surface Features of Recombinant Spider Silk Protein eADF4(κ16)‐Made Materials are Well‐Suited for Cardiac Tissue Engineering

2017 ◽  
Vol 27 (36) ◽  
pp. 1701427 ◽  
Author(s):  
Jana Petzold ◽  
Tamara B. Aigner ◽  
Filip Touska ◽  
Katharina Zimmermann ◽  
Thomas Scheibel ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Spider Silk ◽  
Cardiac Tissue ◽  
Cardiac Tissue Engineering ◽  
Silk Protein ◽  
Surface Features ◽  
Spider Silk Protein

Elastic theory of single spider silk protein molecule

2003 ◽  
Vol 438-439 ◽  
pp. 382-385 ◽  
Author(s):  
Luru Dai ◽  
Yong Zhang ◽  
Zhong-can Ou-Yang
Keyword(s):  
Spider Silk ◽  
Protein Molecule ◽  
Silk Protein ◽  
Elastic Theory ◽  
Spider Silk Protein

scholarly journals Spider silk protein structure analysis by FTIR and STXM spectromicroscopy techniques

2014 ◽  
Vol 2014 (1) ◽  
pp. 35-42 ◽  
Author(s):  
J. Normandeau ◽  
C. Van Kessel ◽  
D. Nicholson ◽  
B. Rahusaar Routledge ◽  
A. Fawcett ◽  
...  
Keyword(s):  
Protein Structure ◽  
Structure Analysis ◽  
Spider Silk ◽  
Silk Protein ◽  
Protein Structure Analysis ◽  
Spider Silk Protein

scholarly journals Microwave Assisted Sol-Gel Synthesis of Silica-Spider Silk Composites

Molecules ◽  
2019 ◽  
Vol 24 (14) ◽  
pp. 2521
Author(s):  
Abul Bashar Mohammad Giasuddin ◽  
David W. Britt
Keyword(s):  
Aqueous Solution ◽  
Infrared Spectroscopy ◽  
Conformational Changes ◽  
Protein Interactions ◽  
Spider Silk ◽  
Sol Gel ◽  
Silk Protein ◽  
Acidic Aqueous Solution ◽  
Silica Nanocomposites ◽  
Spider Silk Protein

This study introduces a simple and environmentally friendly method to synthesize silica-protein nanocomposite materials using microwave energy to solubilize hydrophobic protein in an aqueous solution of pre-hydrolyzed organo- or fluoro-silane. Sol-gel functionality can be enhanced through biomacromolecule incorporation to tune mechanical properties, surface energy, and biocompatibility. Here, synthetic spider silk protein and organo- and fluoro-silane precursors were dissolved and mixed in weakly acidic aqueous solution using microwave technology. Scanning electron microscopy (SEM) and Atomic force microscopy (AFM) images revealed the formation of spherical nanoparticles with sizes ranging from 100 to 500 nm depending, in part, on silane fluoro- or organo-side chain chemistry. The silane-protein interaction in the nanocomposite was assessed through infrared spectroscopy. Deconvoluted ATR-FTIR (Attenuated total reflectance Fourier-transform infrared spectroscopy) spectra revealed silane chemistry-specific conformational changes in the protein-silane nanocomposites. Relative to microwave-solubilized spider silk protein, the β structure content increased by 14% in the spider silk-organo-silica nanocomposites, but decreased by a net 20% in the spider silk-fluoro-silica nanocomposites. Methods of tuning the secondary structures, and in particular β-sheets that are the cross-linking moieties in spider silks and other self-assembling fibrillar proteins, may provide a unique means to promote protein interactions, favor subsequent epitaxial growth process, and enhance the properties of the protein-silane nanocomposites.

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