Hydration of human and bovine serum albumin complexes with chlorophyllin investigated by differential ehf dielectrometry
Keywords:
serum albumin, chlorophyllin, serum albumin-chlorophyllin complex, hydration, EHF dielectrometry
Abstract
This study is designed to examine the hydration effects accompanying the interaction between
chlorophyllin (CHLN), a potent inhibitor of experimental carcinogenesis, and human and bovine serum
albumins (HSA and BSA) in aqueous solutions using differential dielectric method. This method allows
studying both dielectric characteristics and hydration of the compounds under investigation. We show
that for both complexes the process of complex formation is accompanied by changes of dielectric
parameters. We also present calculations of the hydration of proteins and their complexes with ligand,
which were carried out basing on the model concepts. We found that formation of CHLN complex with
fatty acids free BSA is accompanied by a significant decrease of hydration while no notable hydration
changes takes place upon formation of CHLN complex with HSA containing fatty acids. The former
effect indicates that redistribution of free and bound water molecules takes place during the formation of
the complex. The possible causes of effects observed are discussed.
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References
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2. Mancera R. L. Molecular modeling of hydration in drug design / R. L. Mancera // Curr. Opin. Drug Disc. Dev. – 2007. – V. 10(3). – P. 275–280.
3. Analysis of ligand-bound water molecules in high-resolution crystal structures of protein-ligand complexes / Y. Lu., R. Wang, C.-Y. Yang, S. Wang // J. Chem. Inf. Model. – 2007. – V. 47. – P. 668–675.
4. Jana M. Conformational flexibility of a protein–carbohydrate complex and the structure and ordering of surrounding water / M. Jana, S. Bandyopadhyay // Phys. Chem. Chem. Phys. – 2012. – V. 14. – P. 6628–6638.
5. Poornima C.S. Hydration in drug design 3. Conserved water molecules at the ligand-binding sites of homologous proteins / C. S. Poornima, P. M. Dean // J. Comput.-Aided Mol. Des. – 1995. – V. 9. – P. 521–531.
6. Panigrahi S. K. Strong and weak hydrogen bonds in the protein–ligand interface / S. K. Panigrahi, G. R. Desiraju // Proteins: structure, function and bioinformatics. – 2007. – V. 67. – P. 128–141.
7. Poornima C. S. Hydration in drug design 1. Multiple hydrogen-bonding features of water molecules in mediating protein-ligand interactions / C. S. Poornima, P. M. Dean // J. Comput.-Aided Mol. Des. – 1995. – V. 9. – P. 500–512.
8. Mancera R. L. De novo ligand design with explicit water molecules: an application to bacterial neuraminidase / R. L. Mancera // J. Comput.-Aided Mol. Des. – 2002. – V. 16. – P. 479–499.
9. Rarey M. The particle concept: placing discrete water molecules during protein-ligand docking predictions / M. Rarey, B. Kramer, T. Lengaure // Proteins. – 1999. – V. 34. – P. 17–28.
10. Hydration changes under complexation of DNA with some intercalators / O. V. Khorunzhaya, V. A. Kashpur, D. A. Pesina, V. Ya. Maleev // Biophys. Bull. Kharkiv Univ. – 2010. – V. 24 (1). – P. 5–13.
11. Kragh-Hansen U. Practical aspects of the ligand-binding and enzymatic properties of human serum albumin / U. Kragh-Hansen, V. T. G. Chuang, M. Otagiri // Biol. Pharm. Bull. – 2002. – V. 25(6). – P. 695–704.
12. Human serum albumin: from bench to bedside / G. Fanali, A. di Massi, V. Trezza [et al.] // Mol. Asp. Med. – 2012. – V. 33. – P. 209–290.
13. Ouameur A. A. Human Serum albumin complexes with chlorophyll and chlorophyllin / A. A. Ouameur, R. Marty, H. A. Tajmir-Riahi // Biopolymers. – 2005. – V. 77(3). – P.129–136.
14. Tumolo T. Copper chlorophyllin: a food colorant with bioactive properties? / T. Tumolo, U. M. Lanfer-Marquez // Food Res. Int. – 2012. – V. 46. – P. 451–459.
15. Dietary chlorophyllin is a potent inhibitor of aflatoxin B1 hepatocarcinogenesis in rainbow trout / V. Breinholt, J. Hendricks, C. Pereira [et al.] // Cancer Res. – 1995. – V. 55. – P. 57–62.
16. Spectroscopic study on interaction of bovine serum albumin with sodium magnesium chlorophyllin and its sonodynamic damage under ultrasonic irradiation / J. Wang, L. Liu, B. Liu [et al.] // Spectrochimica Acta Part A. – 2010. – V. 75. – P. 366–374.
17. Khorunzhaya O. V. Hydration of DNA complexes with polyamines / O. V. Khorunzhaya, V. A. Kashpur, V. Ya. Maleev // Biophys. Bull. Kharkiv Univ. – 2009. – V. 22 (1). – P. 5–13.
18. Kashpur V. A. Investigation of globular protein hydration by a differential dielectrometric method / V. A. Kashpur, V. Ya. Maleev, T. Yu. Shchegoleva // Mol. Biol. – 1976. – V. 10 (3). – P. 568–575.
19. Hippel A. P. Dielectrics and waves / A. P. Hippel ; transl. from Eng. – Moscow : Foreign literature publishing. – 1960. – 439p.
20. Ellison W. J. Water: a dielectric reference / W. J. Ellison, K. Lamkaouchi, J.-M. Moreau // J. Molec. Liquids. – 1996. – V.68. – P.171–279.
21. Buchanan T. J. The dielectric estimation of protein hydration / T. J. Buchanan, G. M. Haggis, J. B. Hasted // Proc. Roy. Soc. – 1952. – V. A213. – P. 379–391.
22. Dielectric relaxation time and structure of bound water in biological materials / S. Mashimo, S. Kuwabara, S. Yagihara [et al.] // J. Phys. Chem. – 1987. – V. 91. – P. 6337–6338.
23. Hunter M. J. The partial specific volume of bovine plasma albumin in the presence of potassium chloride / M. J. Hunter // J. Phys. Chem. – 1967. – V. 71 (12). – P. 3717–3721.
24. Putnam F. W. The plasma proteins / F. W. Putnam // 2nd Ed., Academic Press, New York. – 1975. – V. 1. – P. 133–181.
25. Hasted J. B. Dielectric properties of aqueous ionic solutions / J. B. Hasted, R. M. Ritson, C. H. Collie // J. Chem. Phys. – 1948. – V. 16 (1). – P. 1–11.
26. Durshlag H. Modeling the hydration of proteins: prediction of structural and hydrodynamic parameters from X-ray diffraction and scattering data / H. Durshlag, P. Zipper // Eur. Biophys. J. – 2003. – V. 32. – P. 487–502.
27. Suzuki M. Hydration study of proteins in solution by microwave dielectric analysis / M. Suzuki, J. Shigematsu, T. Kodama // J. Phys. Chem. – 1996. – V. 100. – P. 7279–7282.
28. Spectroscopic studies on interaction and sonodynamic damage of metallochlorophyllin (Chl-M (M = Fe, Zn and Cu)) to protein under ultrasonic irradiation / J. Gao, Z. Wang, J. Wang [et al.] // Spectrochimica Acta Part A. – 2011. – V. 79. – P. 849–857.
29. Fujiwara S. Steric and allosteric effects of fatty acids on the binding of warfarin to human serum albumin revealed by molecular dynamics and free energy calculations / S. Fujiwara, T. Amisaki // Chem. Pharm. Bull. – 2011. – V. 59(7). – P. 860–867.
30. The effects of drug complexation on the stability and conformation of human serum albumin / A. A. Ouameur, S. Diamantoglou, M. R. Sedaghat-Herati [et al.] // Cell Biochem Biophys. – 2006. – V. 45. – P. 203–213.
31. Spector A. A. Binding of long-chain fatty acids to bovine serum albumin / A. A. Spector, K. John, J. E. Fletcher // J. Lip. Res. – 1969. – V. 10. – P. 56–67.
32. Structural basis of the drug-binding specificity of human serum albumin / J. Ghuman, P. A. Zunszain, I. Petipas [et al.] // J. Mol. Biol. – 2005. – V. 353. – P. 38–52.
33. A molecular dynamics study of human serum albumin binding sites / R. Artali, G. Bombieri, L. Calabi, A. Del Pra // Il Farmaco. – 2005. – V. 60. – P. 485–495.
34. Fang Y. Structural changes accompanying human serum albumin's binding of fatty acids are concerted / Y. Fang, G. C. Tong, G. E. Means // Biochim. Biophys. Acta. – 2006. – V. 1764. – P. 285–291.
35. Crystal structural analysis of human serum albumin complexed with hemin and fatty acid / P. A. Zunszain, J. Ghuman, T. Komatsu [et al.] // BMC Struct. Biol. – 2003. – V. 3. – P. 6–14.
36. Investigation on the site-selective binding of bovine serum albumin by erlotinib hudrochloride / Y. Liu, M. Chen, Z. Luo [et al.] // J. Biomol. Struct. Dyn. – 2013. – V. 31 (10). – P. 1160–1174.
Cited
How to Cite
Pesina, D. A., Kashpur, V. A., Khorunzhaya, O. V., & Shestopalova, A. V. (1). Hydration of human and bovine serum albumin complexes with chlorophyllin investigated by differential ehf dielectrometry. Biophysical Bulletin, 2(30). Retrieved from https://periodicals.karazin.ua/biophysvisnyk/article/view/1593
Section
Molecular biophysics
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