Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties
Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties(410 views) Di Fiore A, Scozzafava A, Winum JY, Montero JL, Pedone C, Supuran CT, De Simone G
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Mar 15; 17(6): 1726-1731.
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Naples, Italy.
Università degli Studi di Firenze, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, I-50019 Sesto Fiorentino, Firenze, Italy
Université Montpellier II, Laboratoire de Chimie Biomoléculaire, UMR 5032, 8 rue de l'Ecole Normale, 34296 Montpellier Cedex, France
Universit degli Studi di Firenze, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, I-50019 Sesto Fiorentino, Firenze, Italy
Universit Montpellier II, Laboratoire de Chimie Biomol culaire, UMR 5032, 8 rue de l'Ecole Normale, 34296 Montpellier Cedex, France
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Eriksson, A.E., Jones, T.A., Liljas, A., (1988) Proteins Struct. Funct., 4, p. 274. , The hCA II-8 complex was obtained by adding a five molar excess of the inhibitor to a 10 mg/mL protein solution in 100 mM Tris-HCl, pH 8.5. The hanging drop vapour diffusion method was used for the crystallization. The drop consisted of 2 μL of the complex solution and 2 μL of the precipitant solution containing 2.5 M (NH4)2SO4, 0.3 M NaCl, 100 mM Tris-HCl (pH 8.4) and 5 mM of 4-(hydroxymercurybenzoate) to improve the crystal quality. Crystals appeared after 2-3 days at 22 °C and were isomorphous to those of the native enzyme belonging to the space group P21 with unit cell parameters of a = 42.07 Å, b = 41.12 Å, c = 72.06 Å and β = 104.51°. X-ray diffraction data were collected at Synchrotron source Elettra in Trieste, using a Mar CCD detector, at 100 K. A cryoprotectant solution was made by inclusion of 15% (v/v) glycerol in the reservoir solution.[...]
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Wilkinson, B. L., Bornaghi, L. F., Houston, T. A., Innocenti, A., Supuran, C. T., Poulsen, S. A., (2006) J. Med. Chem., 49, p. 6539
Eriksson, A. E., Jones, T. A., Liljas, A., (1988) Proteins Struct. Funct., 4, p. 274. , The hCA II-8 complex was obtained by adding a five molar excess of the inhibitor to a 10 mg/mL protein solution in 100 mM Tris-HCl, pH 8. 5. The hanging drop vapour diffusion method was used for the crystallization. The drop consisted of 2 L of the complex solution and 2 L of the precipitant solution containing 2. 5 M (NH4) 2SO4, 0. 3 M NaCl, 100 mM Tris-HCl (pH 8. 4) and 5 mM of 4- (hydroxymercurybenzoate) to improve the crystal quality. Crystals appeared after 2-3 days at 22 C and were isomorphous to those of the native enzyme belonging to the space group P21 with unit cell parameters of a = 42. 07, b = 41. 12, c = 72. 06 and = 104. 51. X-ray diffraction data were collected at Synchrotron source Elettra in Trieste, using a Mar CCD detector, at 100 K. A cryoprotectant solution was made by inclusion of 15% (v/v) glycerol in the reservoir solution. [.]
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Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties
Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties
Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties