Effect of volatile anesthetics on the circular dichroism of bilirubin bound to human serum albumin

McDonagh, Antony F.; Pu, Yu‐Ming; Lightner, David A.

doi:10.1007/bf01930465

Cited by 17 publications

(18 citation statements)

References 21 publications

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“…The average ellipticity values (Fig. 5A) of the peak and trough of the inverted induced-CD spectrum at the optimal CHCI, concentration (40 mM) was in good agreement with data reported previously (McDonagh et al, 1992;Pu et al, 1993). The induced-CD spectrum was reverted to its normal form on removal of chloroform.…”

Section: Figuresupporting

confidence: 90%

“…The inversion of induced-CD spectrum of HSA . bilirubin (McDonagh et al, 1992;Pu et al, 1993;Agati and McDonagh, 1995) and BSA . bilirubin (Fig.…”

Section: Discussionmentioning

confidence: 98%

“…Serum albumins induce biphasic CD spectra in bilirubin Woolley and Hunter, 1970;Beaven et al, 1973;Chen, 1974;Blauer, 1983). Although binding of bilirubin to albumins has been studied for over 25 years by CDhnduced CD, NMR and fluorescence techniques (Blauer andKing, 1968, 1970 ;Blauer, 1983;Agati and McDonagh, 1995;Bonnett et al, 1976Bonnett et al, , 1978Kaplan and Navon, 1983;Lightner et al, 1986;Pal and Patra, 1994a;Patra andPal, 1995, 1996;Tran, 1987;Chen, 1974;Lee and Gillispe, 1981), the exact nature of binding, and the structurelconformation of the bound pigment, in particular the mechanism of inversion of the induced CD spectra Beaven et al, 1973;McDonagh et al, 1992;Pu et al, 1993;Patra andPal, 1995, 1996;Patra, 1996) are not clear.…”

mentioning

confidence: 99%

“…The inversion of induced CD of bilirubin, whether induced by pH Trull et al, 1992a), ionic strength (Blauer and Harmetz, 1972) and anaesthetics (McDonagh et al, 1992;Pu et al, 1993;Patra, 1996) or photoisomerization (Agati and McDonagh, 1995), was restricted to its complex with human serum albumin (HSA). We report here the inversion of induced CD of bilirubin bound to BSA.…”

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confidence: 99%

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Spectroscopic Probes of the Individual and Combined Effects of Triton X‐100 and Chloroform on Serum Albumins and Serum‐Albumin · Bilirubin Complexes

Patra

Pal

1997

European Journal of Biochemistry

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The effects of the non-ionic surfactant Triton X-100 on the biphasic induced CD spectra of bilirubin complexes of human and bovine serum albumins (HSA and BSA) are divergent. While Triton X-100 inverts the induced CD spectrum of HSA . bilirubin, this surfactant enhances the ellipticity values of induced CD of BSA . bilirubin without inversion. The effect of Triton X-100 on the characteristic ultraviolet-CD spectra of the albumins are similar; both the albumins are denatured from their native globular structures. The anionic surfactant SDS, unlike non-ionic Triton X-100, dislodges the ligand from its protein complexes, indicating that both electrostatic and hydrophobic forces are involved in binding of bilirubin to the albumins.The aprotic solvent chloroform inverts the biphasic induced CD spectra of HSA . bilirubin and BSA . bilirubin, whereas CHCI, has relatively little effect on the ultraviolet CD spectra of the albumins. The combined effect of Triton X-I00 and CHCI, shows that the effect of CHCI, predominates over that of Triton X-100. The perturbing effects of Triton X-100 and CHCI, on the CD or induced CD spectra of the proteins or their bilirubin complexes are reversible, and independent of the order in which components were added. The observations suggest that the denaturation of the albumins by Triton X-100 or solvation of CHCI, within albumins markedly alter the internal topography or dynamics of the receptor sites, triggering alterations of the chirality of the bound pigment in sign and/or magnitude.Keywords : bilirubin ; serum albumin ; induced circular dichroism ; enantioselection ; denaturation.Bilirubin, the end product of heme metabolism, is the cytotoxic and neurotoxic pigment of jaundice (Rimington, 1957 ;With, 1968; Brodersen, 1979a;Semba and Kato, 1982;Meisel and Jahr, 1991 ; Ostrow, 1993, 1996;Ostrow et al., 1994;Hansen, 1994). The molecule is a substituted tetrapyrrole dicarboxylic acid. It consists of two dipyrrole halves joined by CH, group. The two dipyrrole halves are intramolecularly hydrogen bonded, between the COOH group of each half and the lactam (NH-C=O) and NH groups of the other half, imposing folded biplanar ridge-tile interconverting enantiomeric conformations (Bonnett et al., 1976(Bonnett et al., , 1978Kaplan and Navon, 1983;Trull et al., 1983Trull et al., , 1987Person et al., 1994;Nogles and Lightner, 1995).Due to the presence of aromatic domains (rings) and imposed conformational restriction, the molecule is hydrophobic in nature, which is unusual for a dicarboxylic acid (Bonnett et al., 1976(Bonnett et al., , 1978 Brodersen, 197913; Lightner and McDonagh, 1984;Lightner et al., 1996). In plasma the pigment is rendered soluble on binding to albumin, the most abundant serum protein, forming a non-covalent-association complex, and is transported to the liver for glucuronidation and subsequent excretion (Ostrow et al., 1963;Cooke and Roberts, 1969; Watson, 1962; Robinson and Rapoport, 1987;Zucker et al., 1994Zucker et al., , 1995. Competitive binding studies with other amphiphi...

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Section: Figuresupporting

confidence: 90%

“…The inversion of induced-CD spectrum of HSA . bilirubin (McDonagh et al, 1992;Pu et al, 1993;Agati and McDonagh, 1995) and BSA . bilirubin (Fig.…”

Section: Discussionmentioning

confidence: 98%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Spectroscopic Probes of the Individual and Combined Effects of Triton X‐100 and Chloroform on Serum Albumins and Serum‐Albumin · Bilirubin Complexes

Patra

Pal

1997

European Journal of Biochemistry

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“…Certain soluble proteins, on the other hand, appear to have a limited number of discrete binding sites for inhalational anesthetics, making them reasonable initial candidates for characterizing anesthetic binding domains. Accordingly, several approaches have identified specific, saturable binding of halothane in bovine serum albumin (3-6) and have also demonstrated anesthetic-induced alterations in the structure or carrier function (7)(8)(9)(10)(11)(12) C]2-bromo-2-chloro-1,1,1-trifluoroethane; 6.6 mCi/mmol) was purchased from DuPont NEN as the neat compound, which was dissolved in buffer as a stock 6 mM solution and stored at Ϫ80°C. Electrophoresis reagents and supplies were purchased from Bio-Rad.…”

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confidence: 99%

Amino Acid Resolution of Halothane Binding Sites in Serum Albumin

Eckenhoff

1996

Journal of Biological Chemistry

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Saturable binding of various inhaled anesthetics to serum albumin has been shown with a variety of approaches. In order to determine the location of halothane binding sites in serum albumin, both human and bovine serum albumins (HSA and BSA) were photolabeled with [ 14 C]halothane, and subjected to proteolysis and microsequencing. BSA was found to have a higher affinity for halothane than HSA, and it contained two specifically labeled sites. One site was characterized by diffuse labeling from Trp 212 -Leu 217, and the other by a more discrete and higher affinity labeling at Trp 134 -Gly 135. HSA contained only a single labeled site, and although lower affinity, was determined to be analogous to BSA Trp 212 . The position 130 -140 region of HSA, having a leucine instead of tryptophan at position 134, was not labeled. These results demonstrate specific and discrete binding of an inhaled anesthetic to a mammaliansoluble protein, and further suggest the importance of aromatic residues as one feature of inhaled anesthetic binding sites.Volatile inhalational anesthetics can bind to and alter the function of a variety of proteins, both soluble and membranebound (1). Determination of the characteristics of these binding sites in proteins should allow prediction of the interactive forces producing binding (immobilization) and also hint at the structural or dynamical consequences to the target. Furthermore, the demonstration of a binding motif common to many protein targets will simplify the search for anesthetic binding domains in other systems. Unfortunately, the character of anesthetic binding sites in protein has been difficult to determine directly, and few examples are available.While consensus places important actions of anesthetics at membrane protein, the presence of lipid and multiple apparently specific binding sites (2) renders these complex models presently unsuitable for a focused search of binding site features. Certain soluble proteins, on the other hand, appear to have a limited number of discrete binding sites for inhalational anesthetics, making them reasonable initial candidates for characterizing anesthetic binding domains. Accordingly, several approaches have identified specific, saturable binding of halothane in bovine serum albumin (3-6) and have also demonstrated anesthetic-induced alterations in the structure or carrier function (7)(8)(9)(10)(11)(12) C]2-bromo-2-chloro-1,1,1-trifluoroethane; 6.6 mCi/mmol) was purchased from DuPont NEN as the neat compound, which was dissolved in buffer as a stock 6 mM solution and stored at Ϫ80°C. Electrophoresis reagents and supplies were purchased from Bio-Rad.Photoaffinity Labeling-Albumin solutions (generally 15 M) in deoxygenated (argon-bubbled) 150 mM NaCl, containing various concentrations (0.05-0.4 mM) of [ 14 C]halothane was exposed to 254 nm light (Oriel Hg pencil calibration lamp at 7 mm) for 60 -100 s in 5-mm path-length quartz cuvettes (2 ml) at 20 -22°C. The final addition completely filled the cuvette, which was then sealed with a Teflon stopper, ...

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Enantioselective inhibition of the binding of rac‐profens to human serum albumin induced by lithocholate

Bertucci

2001

Chirality

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The reversible binding of lithocholate to human serum albumin determines a decrease of the binding of rac-ketoprofen. The process was followed by displacement chromatography using increasing concentrations of the competitor, i.e., lithocholate, in the mobile phase. The inhibition of rac-ketoprofen binding resulting was enantioselective and greater displacement was observed for the (S) enantiomer. The displacement process resulting was competitive in nature, the two enantiomers of ketoprofen binding to the same binding site as the modifier. The investigation was extended to other nonsteroidal antiinflammatory drugs. The enantioselective binding inhibition was larger in the case of rac-naproxen and rac-suprofen with respect to the phenomenon observed in the case of rac-ketoprofen. The difference in circular dichroism spectroscopy was also used to characterize the binding of lithocholate to human serum albumin. This bile acid was proven to bind to site II on human serum albumin. The results, as obtained by displacement chromatography and difference circular dichroism spectroscopy, strongly support the hypothesized role of bile acids in inducing the enantioselective inhibition of ketoprofen binding to human serum albumin in patients suffering from liver diseases.

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Effect of volatile anesthetics on the circular dichroism of bilirubin bound to human serum albumin

Cited by 17 publications

References 21 publications

Spectroscopic Probes of the Individual and Combined Effects of Triton X‐100 and Chloroform on Serum Albumins and Serum‐Albumin · Bilirubin Complexes

Spectroscopic Probes of the Individual and Combined Effects of Triton X‐100 and Chloroform on Serum Albumins and Serum‐Albumin · Bilirubin Complexes

Amino Acid Resolution of Halothane Binding Sites in Serum Albumin

Enantioselective inhibition of the binding of rac‐profens to human serum albumin induced by lithocholate

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