Topic
Human serum albumin
About: Human serum albumin is a research topic. Over the lifetime, 9402 publications have been published within this topic receiving 269029 citations. The topic is also known as: serum albumin & ALB.
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TL;DR: The high concordance between observation and theory favors the Donnan theory and implies that the electrodes are as accurate in a solution with albumin as in a protein-free solution.
Abstract: The ionic activities and total molalities of sodium, potassium, calcium, lithium, and chloride in a solution of human serum albumin were measured at different values of pH between 4 and 9. The same quantities were measured simultaneously in a protein-free electrolyte solution in membrane equilibrium with the albumin solution. Taking the residual liquid-junction potential and bias from unselectivity of the electrodes into account, we determined the own, bound, and net charges of albumin. Chloride was amply bound at low pH, and calcium at high pH. The varying charge of ions bound to albumin opposed the effect of acid or base on the net charge. All ions were distributed across the membrane according to the same electric potential difference, which equalled the Donnan potential. The high concordance between observation and theory favors the Donnan theory and furthermore implies that the electrodes are as accurate in a solution with albumin as in a protein-free solution.
139 citations
TL;DR: Data obtained by fluorescence spectroscopy, CD, and FTIR experiments along with the docking studies suggest that EGCG binds to residues located in subdomains IIa and IIIa of HSA, suggesting that apart from an initial hydrophobic association, the complex is held together by van der Waals interactions and hydrogen bonding.
Abstract: (-)-Epigallocatechin-3-gallate (EGCG), the major constituent of green tea has been reported to prevent many diseases by virtue of its antioxidant properties. The binding of EGCG with human serum albumin (HSA) has been investigated for the first time by using fluorescence, circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, and protein-ligand docking. We observed a quenching of fluorescence of HSA in the presence of EGCG. The binding parameters were determined by a Scatchard plot and the results were found to be consistent with those obtained from a modified Stern-Volmer equation. From the thermodynamic parameters calculated according to the van't Hoff equation, the enthalpy change deltaH degrees and entropy change deltaS degrees were found to be -22.59 and 16.23 J/mol K, respectively. These values suggest that apart from an initial hydrophobic association, the complex is held together by van der Waals interactions and hydrogen bonding. Data obtained by fluorescence spectroscopy, CD, and FTIR experiments along with the docking studies suggest that EGCG binds to residues located in subdomains IIa and IIIa of HSA. Specific interactions are observed with residues Trp 214, Arg 218, Gln 221, Asn 295 and Asp 451. We have also looked at changes in the accessible surface area of the interacting residues on binding EGCG for a better understanding of the interaction.
139 citations
TL;DR: Nonlinear least-squares analysis of the decrease in fluorescence accompanying the displacement yields the stoichiometry and the dissociation constants and is eminently suitable for large-scale screening.
138 citations
TL;DR: Binding of puerarin to human serum albumin was investigated by ultraviolet absorbance, fluorescence, circular dichroism and molecular docking, which suggested the hydrophobic residues such as tyrosine (Tyr) 150, Tyr 148, Tyr 149 and polar residuessuch as lysine (Lys) 199, Lys 195, arginine 257 and histidine 242 played an important role in the binding reaction.
Abstract: Puerarin is a widely used compound in Chinese traditional medicine and exhibits many pharmacological activities. Binding of puerarin to human serum albumin (HSA) was investigated by ultraviolet absorbance, fluorescence, circular dichroism and molecular docking. Puerarin caused a static quenching of intrinsic fluorescence of HSA, the quenching data was analyzed by Stern–Volmer equation. There was one primary puerarin binding site on HSA with a binding constant of 4.12 × 104 M−1 at 298 K. Thermodynamic analysis by Van Hoff equation found enthalpy change (
$$\Delta H^{O} $$
) and entropy change (
$$\Delta S^{O} $$
) were −28.01 kJ/mol and −5.63 J/mol K respectively, which indicated the hydrogen bond and Van der waas interaction were the predominant forces in the binding process. Competitive experiments showed a displacement of warfarin by puerarin, which revealed that the binding site was located at the drug site I. Puerarin was about 2.22 nm far from the tryptophan according to the observed fluorescence resonance energy transfer between HSA and puerarin. Molecular docking suggested the hydrophobic residues such as tyrosine (Tyr) 150, Tyr 148, Tyr 149 and polar residues such as lysine (Lys) 199, Lys 195, arginine 257 and histidine 242 played an important role in the binding reaction.
138 citations
TL;DR: The use of proteins as chiral selectors in CE is reviewed in this article, where the performance of packed-capillary electrochromatography with protein phases is compared with free-solution systems.
138 citations