2021
DOI: 10.1039/d1en00388g
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Interaction of beta-lactoglobulin and bovine serum albumin with iron oxide (α-Fe2O3) nanoparticles in the presence and absence of pre-adsorbed phosphate

Abstract: Protein adsorption onto mineral nanoparticle surfaces is critical to the function and fate of biological compounds in environmental and industrial systems. However, adsorption kinetics, coverage, and conformation of biological macromolecules...

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Cited by 8 publications
(11 citation statements)
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“…Likewise, phosphate pre-adsorption on hematite (α-Fe 2 O 3 )NPs reduces protein surface coverage, slows the protein-specific kinetics of BSA and β-LG, and restricts secondary structural changes in proteins. 94 Phosphate's ability to attenuate the α-Fe 2 O 3 NP-induced secondary structural changes of proteins is attributed to its induction of steric constraints or bridging and ternary complex formation, suggesting phosphate as a potential agent in attenuating adsorbed protein denaturation, particularly at low surface coverage.…”
Section: Biological Factors That Influence Protein Corona Conformationmentioning
confidence: 99%
See 1 more Smart Citation
“…Likewise, phosphate pre-adsorption on hematite (α-Fe 2 O 3 )NPs reduces protein surface coverage, slows the protein-specific kinetics of BSA and β-LG, and restricts secondary structural changes in proteins. 94 Phosphate's ability to attenuate the α-Fe 2 O 3 NP-induced secondary structural changes of proteins is attributed to its induction of steric constraints or bridging and ternary complex formation, suggesting phosphate as a potential agent in attenuating adsorbed protein denaturation, particularly at low surface coverage.…”
Section: Biological Factors That Influence Protein Corona Conformationmentioning
confidence: 99%
“…At pH 6, HM NPs induce protein-specific secondary structural changes in adsorbed BSA and beta-lactoglobulin (β-LG), followed by proteins returning to their solution-phase conformation after 90 minutes. 94 However, phosphate pre-adsorption on HM NPs reduces protein surface coverage, slows the protein-specific kinetics of BSA and β-LG, and restricts secondary structural changes in proteins. The ability of phosphate to attenuate the HM NP-induced secondary structural changes of proteins can be attributed to its induction of steric constraints or bridging and ternary complex formation, suggesting phosphate as a potential agent in attenuating adsorbed protein denaturation, particularly at low surface coverage.…”
Section: Role Of Nanoparticles In Protein Corona Conformationmentioning
confidence: 99%
“…Hydrogen bonding and other nonionic interactions most likely comprise these interactions. [43][44][45] Comparing the BSA and goethite spectrum (light green) in Fig. 3 to that of BSA and goethite alone (Fig.…”
Section: Atr-ftir Spectroscopy Of Multi-component Thin Lmsmentioning
confidence: 99%
“…When Fe 2+ is present in high concentrations, ferrihydrite undergoes a dissolution-recrystallization process to form goethite ( Sheng et al., 2020 ). Phosphate coats the surface of goethite to impede both structural transformations and morphological evolution processes ( Ustunol et al., 2021 ). Both Fe 2+ and PO 4 3- play crucial roles in the growth of rice and the formation of iron plaques ( Giannopolitis and Ries, 1977 ; Amako et al., 1994 ; Sheng et al., 2020 ; Ustunol et al., 2021 ).…”
Section: Introductionmentioning
confidence: 99%