How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site

• Published in: International journal of molecular sciences Vol. 24; no. 4; p. 3659
• Main Authors: Giraudon-Colas, Gaël, Devineau, Stéphanie, Marichal, Laurent, Barruet, Elodie, Zitolo, Andrea, Renault, Jean-Philippe, Pin, Serge
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01-02-2023; MDPI
• Subjects: Absorption spectroscopy; Adsorption; Affinity; Animals; Catalytic Domain; Chemical Sciences; Circular Dichroism; Dichroism; Heme; heme–iron; Hemoglobin; Hemoglobins - chemistry; Hill, Archibald V; Hydrogen bonds; Life Sciences; Ludox (trademark); Nanoparticles; Nanoparticles - chemistry; Oxidation; Protein adsorption; Proteins; Silica; silica nanoparticles; Silicon Dioxide - chemistry; Structure-function relationships; Swine; visible circular dichroism; X ray absorption; X-ray absorption spectroscopy; XAS; France; Germany; adsorption; XAS; silica nanoparticles; hemoglobin; heme–iron; visible circular dichroism
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms24043659

The adsorption of proteins on surfaces has been studied for a long time, but the relationship between the structural and functional properties of the adsorbed protein and the adsorption mechanism remains unclear. Using hemoglobin adsorbed on silica nanoparticles, we have previously shown that hemoglobin's affinity towards oxygen increases with adsorption. Nevertheless, it was also shown that there were no significant changes in the quaternary and secondary structures. In order to understand the change in activity, we decided in this work to focus on the active sites of hemoglobin, the heme and its iron. After measuring adsorption isotherms of porcine hemoglobin on Ludox silica nanoparticles, we analyzed the structural modifications of adsorbed hemoglobin by X-ray absorption spectroscopy and circular dichroism spectra in the Soret region. It was found that upon adsorption, there were modifications in the heme pocket environment due to changes in the angles of the heme vinyl functions. These alterations can explain the greater affinity observed.