Abstract
The effect of a nonsteroidal anti-inflammatory drug, the indomethacin, on the conformation of human serum albumin is investigated by evaluatingα-helix,β-structure and random coil structure contents from optical rotatory dispersion spectra. The observed structural changes may be attributed to theα-helix-to-β-structure conversion, because the content of random coil is not largely changed. The increase inβ-structure is due to a loss in the degrees of freedom in albumin.
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References
Brown JR (1975) Fed Proc 34:591
Aoki K, Foster JF (1956) J Am Chem Soc 79:3538
Wallevik K (1973) J Biol Chem 248:2650
Stroup SD, Foster JF (1973) Biochemistry 12:3824
Kragh-Hansen U (1981) Pharmacol Rev 33:17
Sudlow G, Birkett DJ, Wade DN (1976) Mol Pharmacol 11:824
Rosenor VM, Oratz M, Rothschild MA (1977) In: Brown JR (ed) Albumin Structure, Function and Uses, Pergamon Press, Oxford London, p 27
Solomon HM, Schrogie JJ, Williams D (1968) Biochem Pharmacol 17:143
Hultmark D, Borg KO, Elofsson R, Palmer L (1975) Acta Pharm Suec 12:259
Wood GC, Cooper PF (1970) Chromatog Rev 12:88
Callaghan P, Martin NH (1962) Biochem J 83:144
Greenfield N, Fasman GD (1969) Biochemistry 8:4108
Chen YH, Yang JT, Chau KH (1974) Biochemistry 13:3350
Katz S, Shaw ME, Chillag S, Miller JE (1972) J Biol Chem 247:5228
Blanchard J, Tozer TN, Sorby DL, Tuck LD (1975) Mol Pharmacol 11:133
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Cots, J., Pouplana, R. & Estelrich, J. Conformational changes in the human serum albumin-indomethacin binding. Colloid & Polymer Sci 265, 164–166 (1987). https://doi.org/10.1007/BF01412760
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DOI: https://doi.org/10.1007/BF01412760