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Articles by S.M. Mahbubul Alam
Total Records ( 2 ) for S.M. Mahbubul Alam
  S.M. Mahbubul Alam , Lucky Yeasmin , M. Nadim Reza , J.A. Shilpi , Firoj Ahmed and M. Jamil Akter
  In the current study on Pharmacokinetic parameter of Chloramphenicol especially emphasizing on binding parameters i.e. association constants, number of binding sites, forces involving in the drug-protein interactions was studied by equilibrium dialysis method. Two types of association constants characterize the binding of the drug on BSA: high affinity association constant (k1) with lower number of binding sites (n1) and low affinity association constant (k2) with higher number of binding sites (n2). The values for k1 and k2 at pH 7.4 and at temperature 25 ° C were found (16.9 ± 0.01)x105 and (4.23 ± 0.04)x105 M ha-1 , respectively and those for n1 and n2 were 1.8 ± 0.3 and 4.6 ± 0.4, respectively. Values of k1 were found to decrease both with the increase of pH from 6.4 to 8.4 and temperature from 25 to 40 ° C. Thermodynamic data indicated that the protein-Chloramphenicol binding is exothermic, entropically driven and spontaneous. Electrostatic, hydrogen bonding, vander Waal`s force and hydrophobic interactions are involved in the binding of Chloramphenicol to BSA.
  S.M. Mahbubul Alam , M.M. Rahman , M.H. Rahman and N.N. Rahman
  The interaction of tetracycline hydrochloride to Bovine Serum Albumin (BSA) at various temperatures and pH values using Equilibrium Dialysis (ED) method was studied. Scatchard analysis of the binding data revealed the presence of one high affinity binding site with k1 value of 1.67x106 M-1 and six low affinity binding sites with k2 value of 1.44x105 M-1 at pH 7.4 and 25°C. Site-specific probe displacement data suggested that warfarin site (site-I) is the high affinity binding site and benzodiazepine site (site-II) is the low affinity binding site on BSA for this drug. The high affinity binding site was found to be affected by temperature and pH of the medium. The thermodynamic data indicated that the binding process of tetracycline hydrochloride to BSA is spontaneous, exothermic and entropically driven. Electrostatic forces, hydrogen bonding, hydrophobic interactions and van der Waals forces are probably involved in the overall binding process of tetracycline hydrochloride to BSA. The affinity of this drug to BSA is dependent on the conformational changes of BSA caused by N-B transition.
 
 
 
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