Interactions at the silica-peptide interface: influence of the extent of functionalization on the conformational ensemble

Sola-Rabada, A., Michaelis, M., Oliver, D.J., Roe, M., Colombi Ciacchi, L., Heinz, H. and Perry, C.C. ORCID: 0000-0003-1517-468X, 2018. Interactions at the silica-peptide interface: influence of the extent of functionalization on the conformational ensemble. Langmuir. ISSN 0743-7463

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Abstract

In this contribution, the effect of silica particle size (28 and 210 nm) and surface chemistry (i.e. hydroxyl, methyl or amino groups) on peptide binding response is studied with a specific emphasis on the effect of extent of functionalization on binding. Exhaustive characterization of the silica surfaces was crucial for knowledge of the chemistry and topography of the solid surface under study; and thus, to understand their impact on adsorption and the conformational ensemble of the peptides. The extent of surface functionalization was shown to be particle-size dependent, a higher level of 3-aminopropyl functionality being obtained for smaller particles, while a higher degree of methyl group functionality was found on the larger particles. We demonstrated that peptide interactions at the aqueous interface were not only influenced by the surface chemistry but by the extent of functionalization where a 'switch' of peptide adsorption behavior was observed, while changes in the conformational ensemble revealed by circular dichroism were independent of the extent of functionalization. In addition to electrostatic interactions and hydrogen bonding driving interaction at the silica-peptide interface the data obtained suggested that stronger interactions such as hydrophobic and/or covalent interactions may moderate interaction. The insights gained from this peptide-mineral study give a more comprehensive view of mechanisms concerning mineral-peptide interactions which may allow for the design and synthesis of novel (nano)materials with properties tailored for specific applications.

Item Type:	Journal article
Publication Title:	Langmuir
Creators:	Sola-Rabada, A., Michaelis, M., Oliver, D.J., Roe, M., Colombi Ciacchi, L., Heinz, H. and Perry, C.C.
Publisher:	American Chemical Society
Date:	20 June 2018
ISSN:	0743-7463
Identifiers:	Number Type 10.1021/acs.langmuir.8b00874 DOI
Divisions:	Schools > School of Science and Technology
Record created by:	Linda Sullivan
Date Added:	29 Jun 2018 14:02
Last Modified:	31 Jan 2019 11:01
URI:	https://irep.ntu.ac.uk/id/eprint/33957

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