作者: M. Maciążek-Jurczyk , A. Sułkowska , B. Bojko , J. Równicka , W.W. Sułkowski
DOI: 10.1016/J.MOLSTRUC.2008.12.023
关键词: Methotrexate 、 Drug 、 Plasma protein binding 、 Pharmacology 、 Biochemistry 、 Chemistry 、 Phenylbutazone 、 Quenching (fluorescence) 、 Binding site 、 Serum albumin 、 Albumin
摘要: Abstract Combination of several drugs is often necessary especially during long-them therapy. The competition between can cause a decrease the amount drug bound to albumin. This results in an increase free, biological active fraction drug. aim presented study was describe phenylbutazone (Phe) and methotrexate (MTX), two recommended for treatment rheumatology binding bovine (BSA) human (HSA) serum albumin high affinity site. Fluorescence analysis used estimate effect on protein fluorescence define quenching properties drugs–serum complexes. displacement one from complex other with has been described basis comparison curves constants binary ternary systems. conclusion that both Phe MTX form site same subdomain (IIA) points necessity using monitoring therapy owning possible uncontrolled toxic effects.