Studies on coumarin anticoagulant drugs. Heat of interaction of sodium warfarin and human plasma albumin by heatburst microcalorimetry.
نویسندگان
چکیده
The heat of interaction of sodium warfarin and human plasma albumin has been studied by heatburst microcalorimetry. Sixteen experiments were performed at warfarin concentrations of 0.02 and 0.10% and albumin concentrations of 0.2 and 0.4%. The average heat evolved was -3.14 kcal per mole of warfarin. It is suggested that the molecular basis of the warfarin-albumin interaction is hydrogen and hydrophobic bonding. Microcalorimetry was an ideal method for studying this interaction; the lack of specificity of the thermal method should allow its application to a wide variety of interactions of biological interest.
منابع مشابه
Studies on the coumarin anticoagulant drugs: interaction of human plasma albumin and warfarin sodium.
In studies by continuous flow electrophoresis the coumarin anticoagulant drug warfarin sodium was found to be bound solely to the albumin fraction of the plasma proteins. The interaction was studied in detail by equilibrium dialysis of solutions of crystalline human plasma albumin and warfarin sodium. Analysis of the data showed that albumin possesses a single strong binding site for warfarin w...
متن کاملInteraction of the anticoagulant drug warfarin and its metabolites with human plasma albumin.
The interaction of the anticoagulant drug warfarin and its metabolites with human plasma albumin was studied by equilibrium dialysis. A 20-fold variation of buffer ionic strength (0.017-0.340) caused no significant change in the warfarin association constant. But the binding strength rose significantly as the pH was increased from 6.0 to 9.0 and then declined at pH 10.0. The 6-, 7-, and 8-hydro...
متن کاملBiol. Pharm. Bull. 30(4) 826—829 (2007)
the Sand R-enantiomer, has been used as an anticoagulant agent. The anticoagulant activity of S-warfarin is 3—5 times as great as that of R-warfarin. Warfarin is highly bound to Site I, a warfarin binding site, in the human serum albumin (HSA) molecule (97—99%). The unbound fraction of warfarin is increased by the displacement of the binding site caused by the coadministration of several drugs....
متن کاملStudy of Human Albumin Protein Interaction with Fluorouracil Anticancer Drug Using Molecular Docking Method
Introduction: Drugs are mainly delivered to the target tissues by plasma proteins, such as human serum albumin, in the human body. Practical information about the thermodynamic parameters of drugs and their stability can be obtained using simulation methods, such as molecular docking. Material & Methods: This study, investigated the molecular docking of human serum albumin with fluorouracil an...
متن کاملMolecular dynamics simulation and docking studies on the binding properties of several anticancer drugs to human serum albumin
Disposition and transportation of anticancer drugs by human serum albumin (HSA) affects their bioavailability, distribution and elimination. In this study, the interaction of a set of anticancer drugs with HSA was investigated by molecular dynamics and molecular docking simulations. The drugs' activities were analyzed according to their docking scores, binding sites and structural descriptors. ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 244 5 شماره
صفحات -
تاریخ انتشار 1969