{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["24(4)"],"submitter":["Giraudon-Colas G"],"funding":["Université Paris Saclay"],"pubmed_abstract":["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 an"],"journal":["International journal of molecular sciences"],"pagination":["3659"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9967434"],"repository":["biostudies-literature"],"pubmed_title":["How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site."],"pmcid":["PMC9967434"],"pubmed_authors":["Pin S","Marichal L","Zitolo A","Giraudon-Colas G","Renault JP","Devineau S","Barruet E"],"additional_accession":[]},"is_claimable":false,"name":"How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site.","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 an","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2025-08-24T03:04:06.634Z","creation":"2025-02-18T23:57:44.064Z"},"accession":"S-EPMC9967434","cross_references":{"pubmed":["36835069"],"doi":["10.3390/ijms24043659"]}}