[Study of the interaction between methotrexate and bovine serum albumin by spectrometry].
The interaction of methotrexate (MTX) and bovine serum albumin (BSA) was studied by fluorescence and absorption spectra. The results show that methotrexate strongly quenched the fluorescence of bovine serum albumin, and the quenching mechanism is a static quenching procedure. The binding constants and the number of binding sites between MTX and BSA at different temperatures were calculated. Furthermore, the enthalpy and entropy changes in the interaction were also obtained, and the primary binding pattern between MTX and BSA was interpreted as hydrophobic interaction.
Xie
Wen-jun
WJ
Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China.
Feng
Yu-ping
YP
Cao
Sheng-li
SL
Zhao
Yu-fen
YF
D000818:Animals; D002417:Cattle; D004347:Drug Interactions; D057927:Hydrophobic and Hydrophilic Interactions; D008727:Methotrexate / Q000737:chemistry*; D015394:Molecular Structure; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
D012710:Serum Albumin, Bovine; D008727:Methotrexate