Assoc-Prof. Enrico Ravera, University of Florence, Italy

https://www.cerm.unifi.it/about-us/people/enrico-ravera

"A structural biology view of bioinspired silica"

Similar to natural silaffins and other biological polyamines, hen egg-white lysozyme (HEWL) can promote the formation of condensed silica microparticles without going through the harsh chemical and temperature conditions that are used in the standard sol-gel synthesis. The same chemistry applies to different IV-oxidation state oxides. However, little is known about the reaction mechanism, and even less about the fate of the protein after the reaction. Over the past years, we
applied a wide range of structural biology methodologies to address this curiosity: through X-ray crystallography and molecular simulations we have interrogated the interaction between the protein and the precursor, through MAS-NMR, SAXS and SEM we have characterized  the protein-silica interface, and through EPR spectroscopy we have further investigated this interaction. Collectively, our results indicate that the nature of the protein-precursor interaction is chiefly electrostatic, but the main effect confining the protein within the formed material is steric, even though electrostatics provide orientational preference.