How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site
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 hemogl...
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| Format: | Article |
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MDPI AG
2023-02-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/4/3659 |
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| author | Gaël Giraudon--Colas Stéphanie Devineau Laurent Marichal Elodie Barruet Andrea Zitolo Jean-Philippe Renault Serge Pin |
| author_facet | Gaël Giraudon--Colas Stéphanie Devineau Laurent Marichal Elodie Barruet Andrea Zitolo Jean-Philippe Renault Serge Pin |
| author_sort | Gaël Giraudon--Colas |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-11T08:43:15Z |
| format | Article |
| id | doaj.art-ae23656c018d404d85b4abee3f705b10 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T08:43:15Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-ae23656c018d404d85b4abee3f705b102023-11-16T21:03:09ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-02-01244365910.3390/ijms24043659How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active SiteGaël Giraudon--Colas0Stéphanie Devineau1Laurent Marichal2Elodie Barruet3Andrea Zitolo4Jean-Philippe Renault5Serge Pin6Université Paris-Saclay, CEA, CNRS, NIMBE, 91191 Gif-sur-Yvette, FranceUniversité Paris Cité, CNRS, Unité de Biologie Fonctionnelle et Adaptative, 75013 Paris, FranceUniversité Paris-Saclay, CEA, CNRS, NIMBE, 91191 Gif-sur-Yvette, FranceUniversité Paris-Saclay, CEA, CNRS, NIMBE, 91191 Gif-sur-Yvette, FranceSynchrotron SOLEIL, L’Orme des Merisiers, BP 48 Saint Aubin, 91192 Gif-sur-Yvette, FranceUniversité Paris-Saclay, CEA, CNRS, NIMBE, 91191 Gif-sur-Yvette, FranceUniversité Paris-Saclay, CEA, CNRS, NIMBE, 91191 Gif-sur-Yvette, FranceThe 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.https://www.mdpi.com/1422-0067/24/4/3659hemoglobinheme–ironsilica nanoparticlesadsorptionXASvisible circular dichroism |
| spellingShingle | Gaël Giraudon--Colas Stéphanie Devineau Laurent Marichal Elodie Barruet Andrea Zitolo Jean-Philippe Renault Serge Pin How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site International Journal of Molecular Sciences hemoglobin heme–iron silica nanoparticles adsorption XAS visible circular dichroism |
| title | How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site |
| title_full | How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site |
| title_fullStr | How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site |
| title_full_unstemmed | How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site |
| title_short | How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site |
| title_sort | how nanoparticles modify adsorbed proteins impact of silica nanoparticles on the hemoglobin active site |
| topic | hemoglobin heme–iron silica nanoparticles adsorption XAS visible circular dichroism |
| url | https://www.mdpi.com/1422-0067/24/4/3659 |
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