Journal
ACS BIOMATERIALS SCIENCE & ENGINEERING
Volume 3, Issue 11, Pages 2877-2888Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsbiomaterials.6b00236
Keywords
spider silk; silk-silica fusion proteins; biomineralization; sequence-structure relationship; modeling
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Funding
- NIH [U01 EB014976, R01 DE017207]
- Texas Advanced Computing Center [TG-DMR140101, TG-MSS090007]
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Mineralized polymeric biomaterials provide useful options toward mechanically robust systems for some tissue repairs. Silks as a mechanically robust protein-based material provide a starting point for biomaterial options, particularly when combined with silica toward organic inorganic hybrid systems. To further understand the interplay between silk proteins and silica related to material properties, we systematically study the role of three key domains in bioengineered spider silk fusion proteins with respect to beta-sheet formation and mineralization: (i) a core silk domain for materials assembly, (ii) a histidine tag for purification, and (iii) a silicification domain for mineralization. Computational simulations are used to identify the effect of each domain on the protein folding and accessibility of positively charged amino acids for silicification and predictions are then compared with experimental data. The results show that the addition of the silica and histidine domains reduces beta-sheet structure in the materials, and increases solvent-accessible surface area to the positive charged amino acids, leading to higher levels of silica precipitation. Moreover, the simulations show that the location of the charged biomineralization domain has small effect on the protein folding and consequently surface exposure of charged amino acids. Those surfaces display correlation with the amount of silicification in experiments. The results demonstrate that the exposure of the positively charged amino acids impacts protein function related to mineralization. In addition, processing parameters (solvating agent, the method of beta-sheet induction and temperature) affect protein secondary structure, folding and function. This integrated modeling and experimental approach provides insight into sequence structure function relationships for control of mineralized protein biomaterial structures.
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