The interaction of serum albumin with ethanol

Rosenberg, Robert M.; Rogers, Donald W.; Haebig, Jon E.; Steck, Theodore L.

doi:10.1016/0003-9861(62)90105-4

Cited by 12 publications

(4 citation statements)

References 20 publications

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“…Ethanol serves as a reference cosolvent because it is well-established that the interaction of ethanol with HSA results in the denaturation of the protein. − The secondary and tertiary structure of the protein is partially lost at ethanol concentrations below 30% (v/v), and the protein is completely denatured at 50% (v/v) of ethanol . Furthermore, 13 C NMR spectroscopy demonstrated ethanol-induced changes of the activity of bovine serum albumin as a consequence of direct binding of ethanol to specific hydrophobic binding sites, for example, the FA binding sites .…”

Section: Resultsmentioning

confidence: 99%

Effect of Ionic Liquids on the Solution Structure of Human Serum Albumin

2011

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The effect of several ionic liquids (ILs) on the solution structure of human serum albumin (HSA) is revealed by continuous wave electron paramagnetic resonance (EPR) spectroscopy and nanoscale distance measurements with double electron-electron resonance (DEER) spectroscopy. HSA, the most abundant protein in human blood, is able to bind and transport multiple fatty acids (FAs). Using spin-labeled FA, the uptake of the FA by the protein and their spatial distribution in the protein can be monitored. The FA distribution provides an indirect yet effective way to characterize the structure of the protein in solution. Addition of imidazolium-based ILs to an aqueous solution of HSA/FA conjugates is accompanied by significant destabilization and unfolding of the protein's tertiary structure. In contrast, HSA maintains its tertiary structure when choline dihydrogenphosphate (dhp) is added. The comparison of FA distance distributions in HSA with and without choline dhp surprisingly revealed that with this IL, the FA anchoring units are in better agreement with the crystallographic data. Furthermore, the FA entry point distribution appears widened and more asymmetric than in pure buffer. These results indicate that choline dhp as a cosolvent may selectively stabilize HSA conformations closer to the crystal structure out of the overall conformational ensemble.

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Section: Resultsmentioning

confidence: 99%

Effect of Ionic Liquids on the Solution Structure of Human Serum Albumin

2011

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“…Ha et al (25) showed that ethanol could displace drugs such as warfarin from HSA. However, Rosenberg et al (23) showed no effect of ethanol on the binding of methyl orange to HSA. The effect of methanol will be less than that of ethanol (20).…”

Section: Discussionmentioning

confidence: 98%

“…Alcohols have a large effect on albumin in acid solution, promoting R-helix formation. However, the effects at neutral pH are small (23). Lubas et al (20) showed a weak interaction of methanol with albumin, through the methylene group.…”

Section: Discussionmentioning

confidence: 99%

Applications of Tailored Ferrocenyl Molecules as Electrochemical Probes of Biochemical Interactions

et al. 2006

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The development of electrochemical probes useful for investigating the occupancy by other molecules of sites on complex proteins such as human serum albumin (HSA) is described. Ferrocenyl-(oxoethylene)-fatty acid compounds of different fatty acid chain length probed different binding sites on HSA. The interaction could be changed from one primarily with a drug binding site, when the probe was ferrocene methanol, to one predominantly with medium-chain fatty acid binding sites, by adding an (oxoethylene)-fatty acid substituents. Finally, the interaction could be changed to one interacting primarily with high-affinity long-chain fatty acid binding sites, as the fatty acid chain length in ferrocene-(oxoethylene)-fatty acid molecules increased. These results strongly implied that the binding could be further tailored by relatively simple modifications to the probe, for example, by changing the balance of hydrophobicity and hydrophilicity. The possibility of a procedure using mass-produced electrochemical cells to determine the fractional occupancy of different sites on HSA is demonstrated.

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“…From this evidence and the results of kinetic measurements and studies in the ultracentrifuge, it was concluded that I and II represented structurally different forms of the same enzyme. Thus Hartley, Peterson & Sober (1962) isolated on diethylaminoethylcellulose a number of isomers of crystalline bovine serum albumin differing in the number and degree of oxidation of their thiol groups and were able to produce such isomers by treatment of the solid protein with ethanol, and Rosenberg, Rogers, Haebig & Steck (1962) have shown that, when aqueous solutions of albumin are treated with ethanol, hydrophobic bonds may be broken and the molecule expanded. Since the enzyme being studied has similar solubility properties, a similar mobility on electrophoresis, and most probably a molecular weight similar to that of serum albumin, it seems likely that the low pH, exposure to air and 1963 460 exposure to the conditions on the colurmn might have been sufficient to bring about mild structural changes in the 'albumin-like' molecule of the enzyme without loss of its catalytic activity.…”

Section: Discussionmentioning

confidence: 99%