Interaction of Bisphenol A with Bovine Hemoglobin Using Spectroscopic and Molecular Modeling Methods
Applied Spectroscopy, Vol. 65, Issue 11, pp. 1250-1253 (2011)
Acrobat PDF (779 KB)
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 × 105 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.
Virtual Issues
Vol. 7, Iss. 1 Virtual Journal for Biomedical Optics
Citation
Xiaoyan Fang, Shutao Cao, and Rutao Liu, "Interaction of Bisphenol A with Bovine Hemoglobin Using Spectroscopic and Molecular Modeling Methods," Appl. Spectrosc. 65, 1250-1253 (2011)
http://www.opticsinfobase.org/as/abstract.cfm?URI=as-65-11-1250
You do not have subscription access to this journal. Citation lists with outbound citation links are available to subscribers only. You may subscribe either as an OSA member, or as an authorized user of your institution.
Contact your librarian or system administrator
or
Log in to access OSA Member Subscription
You do not have subscription access to this journal. Cited by links are available to subscribers only. You may subscribe either as an OSA member, or as an authorized user of your institution.
Contact your librarian or system administrator
or
Log in to access OSA Member Subscription
« Previous Article | Next Article »
OSA is a member of 