2011
DOI: 10.1016/j.jlumin.2011.06.005
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Structural analysis and binding domain of albumin complexes with natural dietary supplement humic acid

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Cited by 15 publications
(4 citation statements)
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“…Overall, the fluorescence spectroscopy indicates that the binding of the gold complexes to the HSA proceeds through a single interaction mode that strongly affects the protein emission, consistent with the formation of a non-fluorescent 1:1 adduct in the Overall, the fluorescence spectroscopy indicates that the binding of the gold complexes to the HSA proceeds through a single interaction mode that strongly affects the protein emission, consistent with the formation of a non-fluorescent 1:1 adduct in the ground state for all complexes, except for the complex [P][AuSEt(=Se)] which seems to form a non-fluorescent 1:2 adduct. The binding constants determined for these four complexes are higher than that found for Cisplatin (10 2 M −1 ) and similar to those found for other gold complexes (10 3 −10 4 M −1 ) [67][68][69][70][71].…”
Section: Gold-complexes-hsa Interaction Studiessupporting
confidence: 82%
“…Overall, the fluorescence spectroscopy indicates that the binding of the gold complexes to the HSA proceeds through a single interaction mode that strongly affects the protein emission, consistent with the formation of a non-fluorescent 1:1 adduct in the Overall, the fluorescence spectroscopy indicates that the binding of the gold complexes to the HSA proceeds through a single interaction mode that strongly affects the protein emission, consistent with the formation of a non-fluorescent 1:1 adduct in the ground state for all complexes, except for the complex [P][AuSEt(=Se)] which seems to form a non-fluorescent 1:2 adduct. The binding constants determined for these four complexes are higher than that found for Cisplatin (10 2 M −1 ) and similar to those found for other gold complexes (10 3 −10 4 M −1 ) [67][68][69][70][71].…”
Section: Gold-complexes-hsa Interaction Studiessupporting
confidence: 82%
“…Encapsulation of trypsin and ribonuclease A, which to the contrary bear negatively charged surfaces, suggested that hydrophobic effects can overcome localized charge repulsion when the pH is sufficiently low to reduce surface charge density, fostering entrapment within the HA matrix (Tomaszewski et al, 2011). Encapsulation enhances resistance against proteases (Zang et al, 2000) and preserves activity of soil enzymes, albeit at lower levels, by inducing conformational changes (Ding et al, 2011) and/or hampering access of substrates to the active site (Chen et al, 2004b).…”
Section: Reduction In Infectivity Of Soil Prionsmentioning
confidence: 99%
“…Interaction studies of HSA with biological molecules can elucidate the properties of the drug-protein complex because they may provide useful information about the structural features that determine the therapeutic effectiveness of drugs. Therefore, various studies on the interactions between HSA and small bioactive molecules have been reported over the years [16][17][18][19][20]. Generally, strong binding to HSA will decrease the concentrations of a free drug in plasma, whereas weak binding will reduce the duration of drug action.…”
Section: Introductionmentioning
confidence: 99%