Spectroscopic and molecular modeling studies on the interactions of fluoranthene with bovine hemoglobin.
Spectrochim Acta A Mol Biomol Spectrosc
; 203: 301-307, 2018 Oct 05.
Article
in En
| MEDLINE
| ID: mdl-29879645
ABSTRACT
This study aims to investigate the interaction between fluoranthene (FLA) and Bovine hemoglobin (BHb) by ultraviolet-visible (UV-vis) absorption, fluorescence, synchronous fluorescence, circular dichroism (CD) spectroscopy and molecular docking method. The results showed that the fluorescence intensity of BHb was declined with the increase of FLA concentration. The binding procedure was spontaneous mainly driven by hydrophobic force. The number of binding sites were 0.709 (298â¯K), and 1.41 (310â¯K). The binding constants were equal to 4.68â¯×â¯103â¯mol·L-1 at 298â¯K and 6.17â¯×â¯105â¯mol·L-1 at 310â¯K. The binding distance between FLA and the tryptophan residue of BHb was 4.50â¯nm. The results of UV-vis spectra, synchronous fluorescence and CD spectra revealed that FLA could change the conformation of BHb, which might affect the physiological functions of hemoglobin. Moreover, molecular modeling results showed that the fluorescence experimental results were in agreement with the results obtained by molecular docking.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Spectrum Analysis
/
Hemoglobins
/
Models, Molecular
/
Fluorenes
Limits:
Animals
Language:
En
Journal:
Spectrochim Acta A Mol Biomol Spectrosc
Journal subject:
BIOLOGIA MOLECULAR
Year:
2018
Document type:
Article
Affiliation country:
China