title: Interaction of bisphenol A with bovine hemoglobin using spectroscopic and molecular modeling methods.
abstract: The interaction of bisphenol A with bovine hemoglobin (BHb) under physiological conditions was investigated by using fluorescence, ultraviolet-visible (UV-Vis) absorption, circular dichroism (CD), and molecular modeling. The experimental results showed that BPA can bind with BHb  to form a complex. The binding constant Ka and the number of binding sites n were calculated to be 1.49 × 10(5) L mol(-1) and 1, respectively. Molecular modeling study revealed that BPA bound into BHb central cavity, and the binding mode of BPA-BHb  complex could be hydrogen bonding. The UV-Vis absorption and CD spectra indicated that the secondary structure of BHb was altered, which may affect physiological functions of hemoglobin. This work is helpful for clarifying the molecular toxic mechanism of BPA in vivo.
authors: Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, China-America CRC for Environment and Health, Shandong Province, Jinan 250100, China.
authors: Xiaoyan
authors: X
authors: Fang
authors: Shutao
authors: S
authors: Cao
authors: Rutao
authors: R
authors: Liu
mesh_terms: D000818:Animals; D001559:Benzhydryl Compounds; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism / Q000379:methods*; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010636:Phenols / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet; D000098826:Bisphenol A Compounds
chemical_list: D001559:Benzhydryl Compounds; D006454:Hemoglobins; D010636:Phenols; C006780:bisphenol A; D000098826:Bisphenol A Compounds