Spectroscopic studies on the interactions between 3,4-dihydropyrimidin-2(1H)-ones and bovine serum albumin.
The interactions between 3,4-dihydropyrimidin-2(1H)-ones (DHPM) and bovine serum albumin (BSA) were investigated by fluorescence and ultraviolet spectroscopy under imitated physiological conditions. The experimental results showed that all DHPM could form complexes with BSA. Static quenching and non-radiation energy transfer are the main reasons leading to the fluorescence quenching. The binding constants (K(A)) and the number of binding sites (n) were calculated. According to Förster theory of non-radiation energy transfer, the binding distances (r) between BSA and DHPM are less than 7 nm. The relationship between different aryl groups in pyrimidine ring and the binding ability of DHPM with BSA is preliminarily discussed. Moreover, the synchronous fluorescence spectra indicated that the conformation of BSA has not been changed.
Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201, China.
Xianyong
X
Yu
Ronghua
R
Liu
Danhong
D
Ji
Jian
J
Xie
Fengxian
F
Yang
Xiaofang
X
Li
Haowen
H
Huang
Pinggui
P
Yi
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004735:Energy Transfer; D007700:Kinetics; D008968:Molecular Conformation; D011744:Pyrimidinones / Q000737:chemistry / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry
D011744:Pyrimidinones; D012710:Serum Albumin, Bovine; D014364:Tryptophan