Lysozyme is Sterically Trapped Within the Silica Cage in Bioinspired Silica-Lysozyme Composites: A Multi-Technique Understanding of Elusive Protein-Material Interactions

Francesco Bruno, Lucia Gigli, Giovanni Ferraro, Andrea Cavallo, Vladimir K. Michaelis, Gil Goobes, Emiliano Fratini, Enrico Ravera

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Lysozyme is widely known to promote the formation of condensed silica networks from solutions containing silicic acid, in a reproducible and cost-effective way. However, little is known about the fate of the protein after the formation of the silica particles. Also, the relative arrangement of the different components in the resulting material is a matter of debate. In this study, we investigate the nature of the protein-silica interactions by means of solid-state nuclear magnetic resonance spectroscopy, small-angle X-ray scattering, and electron microscopy. We find that lysozyme and silica are in intimate contact and strongly interacting, but their interaction is neither covalent nor electrostatic: lysozyme is mostly trapped inside the silica by steric effects.

Original languageEnglish
Pages (from-to)8030-8037
Number of pages8
JournalLangmuir
Volume38
Issue number26
DOIs
StatePublished - 5 Jul 2022

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