This webinar will focus on the integrated treatment of mineralized polymeric biomaterials, which provide useful options towards mechanically robust systems for some tissue repairs. Silks as a mechanically robust protein-based materials provide a starting point for biomaterial options, particularly when combined with silica towards organic-inorganic hybrid systems. To further understand the interplay between silk proteins and silica related to material properties, we systematically studied the role of three key domains in bioengineered spider silk fusion proteins with respect to mineralization, a core silk domain for materials assembly, a histidine tag for purification, and a silicification domain for mineralization. The goal was to assess these domains with respect to b-sheet formation and biomineralization. Computational simulations were used to identify the effect of each domain on the protein folding and accessibility of positively charged amino acids for silicification and predictions were then compared with experimental data. The results showed that the addition of the silica and histidine domains reduced b-sheet structure in the materials, and increased solvent accessible surface area to the positive charged amino acids, leading to higher levels of silica precipitation. Moreover, the simulations showed that the location of the charged biomineralization domain affected protein folding and consequently surface exposure of charged amino acids. These surface displays correlated with the amount of silicification in experiments. These results demonstrated that the exposure of the positively charge amino acids impacted protein function related to mineralization. In addition, processing parameters (solvating agent, the method of β-sheet induction and temperature) affected 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.

This webinar is hosted by the ImuBEAM WG of the IMAG/MSM Consortium

Meeting Link: https://nih.webex.com/nih/j.php?MTID=m160b25db9f23cebc4410c5196b174f50

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