Binding characteristics of bovine serum albumin encapsulated in sol-gel glasses: an alternative for protein interaction studies |
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Authors: | Vera-Avila Luz E García-Salgado Erika García de Llasera Martha P Peña-Alvarez Araceli |
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Institution: | Departamento de Química Analítica, Facultad de Química, Universidad Nacional Autónoma de México, 04510 México D.F., Mexico. luzelena@servidor.unam.mx |
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Abstract: | Silica glasses doped with 500-700 microg of bovine serum albumin were prepared by the sol-gel method; two pH conditions (pH 5 and 7) were assayed for protein encapsulation. Both biomaterials showed a highly porous structure, with pore sizes in the range 5-28 nm. Columns packed with the ground biogels were on-line coupled to a C18 HPLC column for evaluation of the entrapped protein binding properties using propranolol. Binding capacities (at saturation) were approximately 3.7 and 7.1 microg of propranolol (drug-protein molar ratios 1.4 and 2.7) for the biogels prepared at pH 5 and 7, respectively. The significant difference indicates increased albumin denaturation upon encapsulation at pH 5. A frontal analysis study was then performed in cartridges packed with biogel prepared at pH 7 to evaluate the protein interaction with naproxen at low concentrations (
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Keywords: | Bovine serum albumin Sol-gel-encapsulated proteins Binding characteristics Affinity biogel columns |
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