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

doi:10.1021/acs.langmuir.2c00836

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

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

7 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 language	English
Pages (from-to)	8030-8037
Number of pages	8
Journal	Langmuir
Volume	38
Issue number	26
DOIs	https://doi.org/10.1021/acs.langmuir.2c00836
State	Published - 5 Jul 2022

Bibliographical note

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© 2022 American Chemical Society. All rights reserved.

Funding

This work has been supported by the Fondazione Cassa di Risparmio di Firenze, by the Italian Ministero dell’Istruzione, dell’Università e della Ricerca, through the “Progetto Dipartimenti di Eccellenza 2018–2022” to the Department of Chemistry “Ugo Schiff” of the University of Florence. F.B., G.F., E.F., and E.R. acknowledge the Italian Ministry of Education, University and Research (MIUR), and European Social Fund (ESF) for the PON R&I 2014–2020 program, actions IV.4 “Doctorates and research contracts on Innovation topics” and IV.6 “Research contracts on green issues”. GF and EF acknowledge partial financial support from Consorzio per lo sviluppo dei Sistemi a Grande Interface (CSGI). The authors acknowledge the support and the use of resources of Instruct-ERIC, a landmark ESFRI project, and specifically the CERM/CIRMMP Italy center.

Funders	Funder number
CSGI
Consorzio per lo sviluppo dei Sistemi a Grande Interface
Ente Cassa di Risparmio di Firenze
Ministero dell’Istruzione, dell’Università e della Ricerca
Università degli Studi di Firenze
European Social Fund

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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.",

author = "Francesco Bruno and Lucia Gigli and Giovanni Ferraro and Andrea Cavallo and Michaelis, {Vladimir K.} and Gil Goobes and Emiliano Fratini and Enrico Ravera",

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AU - Gigli, Lucia

AU - Ferraro, Giovanni

AU - Cavallo, Andrea

AU - Michaelis, Vladimir K.

AU - Goobes, Gil

AU - Fratini, Emiliano

AU - Ravera, Enrico

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

Abstract

Bibliographical note

Funding

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