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Discover Supplement-Drug Interactions
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Last Updated: 3 years ago
supplement:
Serum Albumin, Human
Research Papers that Mention the Interaction
“ThT fluorescence kinetic studies indicated that SDS at low concentrations induced more fibrillation of HSA , while SDS at high concentrations inhibited the fibrillation of HSA.”
“Thus, SDS acts as a salt at lower concentrations, while at higher concentrations acts as a chaperon, with significant impact on fibrillation of HSA.”
Sodium dodecyl sulphate modulates the fibrillation of human serum albumin in a dose-dependent manner and impacts the PC12 cells retraction.“The study of circular dichroism spectra demonstrated that the presence of NADs decreased the α-helical content of HSA and induced the change of the secondary structure of HSA.”
“Both fluorescence intensity and lifetimes of HSA decreased with the increasing concentration of SDS , and the surfactant molecules serve the role of a quencher for the fluorescence of Trp214.”
“Binding of SDS to HSA is found to accelerate the solvation dynamics approximately 1.3-fold.”
“Study of HSA-SDS (sodium dodecyl sulphate) interaction at … degrees C and 35 degrees C reveals that SDS affects the HSA structure at least in three steps: the first two steps result in more stabilization and compactness of HSA structure, while the last one induces the unfolding of HSA.”
“… HSA has a … for SDS at 45 degrees C compared to 35 degrees C, It is suggested that the net negative charge of HSA is decreased in …, which results in the decrease of HSA-associated cations and plasma osmolarity, and consequently, heat removal via the increase in urine volume.”
“Selective precipitation with SDS produces enhancements in IL-4 over HSA of more than 2000-fold.”
“This was further confirmed by a stronger desorption of HSA following sodium dodecyl sulfate (SDS) treatment on the CH3 surface compared to the COOH surface.”
“While maintaining specificity for albumin, we reduced the reaction difference between HMA and HNA, with the addition of sodium dodecylsulfate and 5,5'-dithiobis(2-nitrobenzoic acid) to the BCP reagent.”
“Binding of sodium dodecyl sulfate (SDS) to bovine serum albumin (BSA) and human serum albumin ( HSA ) in aqueous solutions at room temperature induces significant changes in the phosphorescence lifetime of tryptophan (Trp) residues.”
“The binding is high affinity and limited capacity due to both, ionic and hydrophobic interactions between HSA and SDS.”
Application of maximum bubble pressure surface tensiometer to study protein-surfactant interactions.
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