Studies on the interaction between Oxaprozin-E and bovine serum albumin by spectroscopic methods.
The interaction between Oxaprozin-E and bovine serum albumin (BSA) was studied by spectroscopic methods including fluorescence and UV-vis absorption spectroscopy. The quenching mechanism of fluorescence of BSA by Oxaprozin-E was discussed to be a dynamic quenching procedure. The number of binding sites n and apparent binding constant K was measured by fluorescence quenching method. The thermodynamics parameter DeltaH, DeltaG, DeltaS were calculated. The results indicate the binding reaction was mainly entropy-driven and hydrophobic forces played major role in the binding reaction. The distance r between donor (BSA) and acceptor (Oxaprozin-E) was obtained according to Förster theory of non-radioactive energy transfer.
Sun
Shao-Fa
SF
Department of Chemistry and Life Sciences, Xianning College, Xianning, PR China.
Zhou
Bo
B
Hou
Han-Na
HN
Liu
Yi
Y
Xiang
Guang-Ya
GY
D000818:Animals; D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000737:chemistry; D002417:Cattle; D000077431:Oxaprozin; D011422:Propionates / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
D000894:Anti-Inflammatory Agents, Non-Steroidal; D011422:Propionates; D012710:Serum Albumin, Bovine; D000077431:Oxaprozin