Spectroscopic investigation on the toxicological interactions of 4-aminoantipyrine with bovine hemoglobin.
The effects of 4-aminoantipyrine (AAP) on bovine hemoglobin (BHb) were investigated by fluorescence spectroscopy, synchronous fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy and circular dichroism spectroscopy (CD) under simulated physiological conditions. The experimental results showed that AAP effectively quenched the intrinsic fluorescence of BHb via static quenching. The number of binding sites, the binding constant K(a), and the thermodynamic parameters (DeltaH(o), DeltaS(o) and DeltaG(o)) were measured at two different temperatures. Van der Waals' interactions and hydrogen bonds were the predominant intermolecular forces in stabilizing the BHb-AAP complex. The experiment results confirmed micro-environmental and conformational changes of BHb in the presence of AAP. The alpha-helix content decreased, indicating that AAP destroys some of the hydrogen bonding networks in the polypeptide chain.
Teng
Yue
Y
Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, 27 Shanda South Road, Jinan, 250100, People's Republic of China.
Liu
Rutao
R
Yan
Shifeng
S
Pan
Xingren
X
Zhang
Pengjun
P
Wang
Meijie
M
D000675:Ampyrone / Q000378:metabolism* / Q000633:toxicity*; D000818:Animals; D002417:Cattle; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation / Q000187:drug effects; D013057:Spectrum Analysis; D013816:Thermodynamics
D006454:Hemoglobins; D000675:Ampyrone