Interaction of anesthetic supplement thiopental with human serum albumin

• Authors: Shahper Khan , Barira Islam , M Rajeswari , Hammad Usmani , Asad Khan
• Languages of publication: EN

Abstracts

EN

Thiopental (TPL) is a commonly used barbiturate anesthetic. Its binding with human serum albumin (HSA) was studied to explore the anesthetic-induced protein dysfunction. The basic binding interaction was studied by UV-absorption and fluorescence spectroscopy. An increase in the binding affinity (K) and in the number of binding sites (n) with the increasing albumin concentration was observed. The interaction was conformation-dependent and the highest for the F isomer of HSA, which implicates its slow elimination. The mode of binding was characterized using various thermodynamic parameters. Domain II of HSA was found to possess a high affinity binding site for TPL. The effect of micro-metal ions on the binding affinity was also investigated. The molecular distance, r, between donor (HSA) and acceptor (TPL) was estimated by fluorescence resonance energy transfer (FRET). Correlation between the stability of the TPL-N and TPL-F complexes and drug distribution is discussed. The structural changes in the protein investigated by circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy reflect perturbation of the albumin molecule and provide an explanation for the heterogeneity of action of this anesthetic.

Keywords

EN

thiopental; fluorescence resonance energy transfer; thermodynamics; FT-IR; circular dichroism

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2008
• Volume: 55
• Issue: 2
• Pages: 399-409

Dates

published

2008

received

2007-08-18

revised

2008-01-15

accepted

2008-01-31

(unknown)

2008-02-01

Contributors

author

Shahper Khan

• Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India, Aligarh, India

author

Barira Islam

• Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India, Aligarh, India

author

M Rajeswari

• Department of Biochemistry, All India Institute of Medical Sciences, New Delhi, India, Aligarh, India

author

Hammad Usmani

• Department of Anesthesiology, JN Medical College, AMU, Aligarh, India, Aligarh, India

author

Asad Khan

• Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India, Aligarh, India

References

• Ahmad B, Parveen S, Khan RH (2006) Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: a novel approach directly assigning binding site. Biomacromolecules 7: 1350-1356.
• Aki H, Yamamoto M (1989) Thermodynamics of the binding of phenothiazines to human plasma, human serum albumin and alpha 1-acid glycoprotein: a calorimetric study. J Pharm Pharmacol 41: 674-679.
• Borga O, Borga B (1997) Serum protein binding of nonsteroidal anti-inflammatory drugs: a comparative study. J Pharmacokinet Biopharm 25: 63-77.
• Chamouard JM, Barre J, Urien S, Houin G, Tillement JP (1985) Diclofenac binding to albumin and lipoproteins in human serum. Biochem Pharmacol 34: 1695-1700.
• Chen YH, Yang JT (1971) A new approach to the calculation of secondary structures of globular proteins by optical rotatory dispersion and circular dichroism. Biochem Biophys Res Commun 44: 1285-1291.
• Chmelik J, Kalous V (1982) Polarographic investigation of conformational changes of human serum albumin. Bioelectrochem Bioenerg 9: 7-13.
• Cui F-L, Fan J, Li J-P, Hu Z (2004) Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy. Bioorg Med Chem 12: 151-157.
• Dugaiczyk A, Law SW, Dennison OE (1982) Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc Natl Acad Sci USA 79: 71-75.
• Epps DE, Raub TJ, Caiolfa V, Chiari A, Zamai M (1999) Determination of the affinity of drugs toward serum albumin by measurement of the quenching of the intrinsic tryptophan fluorescence of the protein. J Pharm Pharmacol 51: 41-48.
• Förster T, Sinanoglu O, eds (1996) Modern Quantum Chemistry, p. 93. Academic Press, New York.
• Feng X-Z, Lin, Z, Yang L-J, Wang C, Bai C-L (1998) Investigation of the interaction between acridine orange and bovine serum albumin. Talanta 47: 1223-1229.
• Gao H, Lei L, Liu J, Qin K, Chen X, Hu Z (2004) The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectrophotometric methods. J Photochem Photobiol Part A 167: 213-221.
• Gelamo EL, Silva CHTP, Imasato H, Tabak M (2002) Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modeling. Biochim Biophys Acta 1594: 84-99.
• Giraud O, Dehoux M, Rolland C, Mantz J, Malas V, Toueg ML, Desmonts JM, Aubier M (1998) Differential effects of halothane and thiopental on the lung inflammatory response after LPS-induced lung injury in the rat. Anesthesiology 89: 34-38.
• He W, Li Y, Xue C, Hu Z, Chen X, Sheng F (2005) Effect of Chinese medicine alpinetin on the structure of human serum albumin. Bioorg Med Chem 13: 1837-1845.
• Hu YJ, Liu Y, Wang JB, Xiao XH, Qu SS (2004) Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. J Pharm Biomed Anal 36: 915-919.
• Hu YJ, Liu Y, Shen XS, Fang XY, Qu SS (2005) Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin. J Mol Struct 738: 143-147.
• Jiaquin L, Jianniao T, Zhang J, Hu Z, Xingguo C (2003) Interaction of magnolol with bovine serum albumin: a fluorescence-quenching study. Anal Bioanal Chem 376: 864-867.
• Khan MY (1986) Direct evidence for involvement of domain III in the N-F transition of bovine serum albumin. Biochem J 236: 307-310.
• Khan SN, Islam B, Khan AU (2007) Probing midazolam interaction with human serum albumin and its effect on structural state of protein. Int J Integ Biol 2: 102-112.
• Kragh-Hansen U (1981) Molecular aspects of ligand binding to serum albumin. Pharmacol Rev 33: 17-53.
• Krier C, Wiedemann K, Polarz H (1984) Hazards of high dose barbiturate therapy in head-injury patients. Acta Anaesthesiol Belg 35: 361-369.
• Li Y, He W, Liu J, Sheng F, Hu Z, Chen X (2005) Binding of the bioactive component jatrorrhizine to human serum albumin. Biochim Biophys Acta 1722: 15-21.
• Lloyd JBF (1971) Synchronized excitation of fluorescence. ernission spectra. Nat Phys Sci 231: 64-65.
• Martin BK (1965) Potential effect of the plasma proteins on drug distribution. Nature 207: 274-276.
• Miles JL, Morey E, Crain F, Gross S, San Julian J, Canady WJ (1962) Inhibition of α-chymotrypsin by diethyl ether and certain alcohols: a new type of competitive inhibition. J Biol Chem 237: 1319-1322.
• Miller JN (1979) Recent advances in molecular luminescence analysis. Proc Anal Div Chem Soc 16: 203-208.
• Neault JF, Tajmir-Riahi HA (1998) Interaction of cisplatin with human serum albumin: Drug binding mode and protein secondary structure. Biochem Biophys Acta 1384: 153-159.
• Pang YH, Yang LL, Shuang SM, Dong C, Thompson M (2005) Interaction of human serum albumin with bendroflumethiazide studied by fluorescence spectroscopy. J Photochem Photobiol B 80: 139-144.
• Peters T Jr (1996) All about albumin: biochemistry, genetics and medical application. Academic Press, Inc, NY.
• Rahman MH, Maruyama T, Okada T, Yamasaki K, Otagiri M (1993) Study of interaction of carprofen and its enantiomers with human serum albumin-I. Biochem Pharmacol 46: 1721-1731.
• Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions. Forces contributing to stability. Biochemistry 20: 3096-3102
• Ryan CW, Vogelzang NJ, Vokes EE, Kindler HL, Undevia SD, Humerickhouse R, Andre AK, Wang Q, Carr RA, Ratain MJ (2004) Dose-ranging study of the safety and pharmacokinetics of atrasentan in patients with refractory malignancies. Clin Cancer Res 10: 4406-4411.
• Schalen W, Messeter K, Nordstrom CH (1992) Complications and side effects during thiopentone therapy in patients with severe head injuries. Acta Anaesthesiol Scand 36: 369-377.
• Seedher N, Singh B, Singh P (1999) Mode of interaction of metronidazole with bovine serum albumin. Indian J Pharm Sci 61: 143-148.
• Sereikaite J, Bumelis VA (2006) Congo red interaction with α-proteins. Acta Biochim Polon 53: 87-92.
• Skarlosh VM (1974) Effect of thiopental sodium on the biligenic function of the liver. Farmakol Toksikol 37: 701-702.
• Surewicz WK, Mantsch HH, Chapman D (1993) Determination of protein secondary structure by Fourier-transform infrared spectroscopy: a critical assessment. Biochemistry 32: 389-394.
• Tian JN, Liu JQ, Zhang JY, Hu ZD, Chen XG (2003) Fluorescence studies on the interactions of barbaloin with bovine serum albumin. Chem Pharm Bull 51: 579-582.
• Valeur B, Brochon JC (1999) New Trends in Fluorescence Spectroscopy. 6th edn, p. 25. Springer Press, Berlin.
• Ware WR (1962) Oxygen quenching of fluorescence in solution, an experimental study of the diffusion process. J Phys Chem 66: 455-458.
• Wilting J, Vander Glesen WF, Janssen LH, Weideman MM, Otagiri M, Perrin JH (1980) The dependence of the binding of warfarin to human serum albumin on the hydrogen, calcium and chloride ion concentrations as studied by circular dichroism, fluorescence, and equilibrium dialysis. J Biol Chem 255: 3032-3037.