Human serum albumin interaction with formononetin studied using fluorescence anisotropy, FT-IR spectroscopy, and molecular modeling methods

2006 ◽  
Vol 14 (5) ◽  
pp. 1431-1436 ◽  
Author(s):  
Ying Li ◽  
WenYing He ◽  
YuMing Dong ◽  
Fenling Sheng ◽  
ZhiDe Hu
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Ir Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Anisotropy ◽  
Modeling Methods ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

SPECTROSCOPIC STUDY OF PROPOFOL BINDING TO HUMAN SERUM ALBUMIN

2010 ◽  
Vol 05 (04) ◽  
pp. 209-226 ◽  
Author(s):  
SAQER M. DARWISH
Keyword(s):  
Human Serum Albumin ◽  
Ir Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Secondary Structure ◽  
Complex Molecules ◽  
Ft Ir ◽  
Β Sheets ◽  
Α Helix ◽  
Ft Ir Spectroscopy

The interaction of propofol and human serum albumin (HSA) has been investigated by UV-absorption, fluorescence spectroscopy and Fourier transform infrared (FT-IR) spectroscopy. Propofol has shown a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (k) is estimated at a low value of 2.55 × 103M-1at 293 K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure in the amide regions I, II and III. The observed spectral changes of HSA-propofol complex indicate a larger intensity decrease in the absorption band of α-helix relative to that of β-sheets. This variation in intensity is related indirectly to the formation of H-bonding in the complex molecules, which accounts for the different intrinsic propensities of α-helix and β-sheets.

scholarly journals Insights from a combination of theoretical and experimental methods for probing the biomolecular interactions between human serum albumin and clomiphene

RSC Advances ◽  
2018 ◽  
Vol 8 (71) ◽  
pp. 40663-40675 ◽  
Author(s):  
Seyed Zachariah Moradi ◽  
Sajad Moradi ◽  
Amin Nowroozi ◽  
Komail Sadrjavadi ◽  
Negin Farhadian ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Experimental Methods ◽  
Transport Protein ◽  
Plasma Transport ◽  
Biomolecular Interactions ◽  
Modeling Methods ◽  
Ft Ir

In this study, the interaction of clomiphene with human serum albumin (HSA), the most abundant plasma transport protein, was investigated using spectrofluorometric, FT-IR, UV-Vis, and molecular modeling methods.

scholarly journals Investigation of the mechanism of binding of thiacloprid to human serum albumin using spectroscopic techniques and molecular modeling methods

2011 ◽  
Vol 25 (2) ◽  
pp. 113-122 ◽  
Author(s):  
Chuanxian Wang ◽  
Qinghua Chu ◽  
Changyun Chen ◽  
Zhao Bo
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interactions ◽  
Entropy Change ◽  
Binding Pocket ◽  
Cd Spectroscopy ◽  
Spectroscopic Techniques ◽  
Modeling Methods

Fluorescence spectroscopy, UV absorption, circular dichroism (CD) spectroscopy and molecular modeling methods were used to characterize the binding properties of thiacloprid (TL) with human serum albumin (HSA) at molecular level under physiological conditions. The fluorescence intensity of HSA decreased regularly with the gradually increasing concentration of thiacloprid. The binding constant K at three different temperatures (290, 300 and 310 K) were 3.07, 2.74 and 1.35 × 104M−1, respectively, for TL–HSA interaction have been calculated from the relevant fluorescence data. CD spectroscopic measurements have shown that the secondary structures of the protein have been changed by the interaction of thiacloprid with HSA. Furthermore, the study of molecular modeling indicated that thiacloprid could be located on the surface of the binding pocket of subdomains IIA in HSA. The hydrophobic interaction was the major acting force and there are H-bonds and electrostatic interactions between TL and HSA, which is in good agreement with the results from the experimental thermodynamic parameters (the enthalpy change ΔH0and the entropy change ΔS0were calculated to be -20.378 kJ/mol and 16.328 J/mol K according to the Van9t Hoff equation).

Sign in / Sign up

Export Citation Format

Share Document