化学
人血清白蛋白
分子
牛血清白蛋白
结合位点
结合常数
配体(生物化学)
分子动力学
白蛋白
作者
Hamid Dezhampanah,Roghaye Firouzi,Leila Hasani
出处
期刊:Protein and Peptide Letters
[Bentham Science]
日期:2016-08-31
卷期号:23 (9): 800-807
标识
DOI:10.2174/0929866523666160719101707
摘要
The interaction of nickel tetra sulfunated phthalocyanine( NiTSPc) with
human serum albumin (HSA), in 20 mM phosphate buffer pH 7.4 was investigated
using advanced techniques including fluorescence, synchronous fluorescence,
Fourier transform infrared (FT-IR), circular dichroism (CD) spectroscopy and
molecular docking. The fluorescence quenching measurements showed a single
binding site on HSA for NiTSPc with the binding constant (K b ) value equals to
1.26×106 at 25°C. The results showed that quenching mechanism of HSA by
NiTSPc was of dynamic type. The results from FTIR and CD spectroscopies demonstrated
that NiTSPc binds to amino acid residues of the main polypeptide chain
in protein destroying the hydrogen bonding network. The corresponding thermodynamic
parameters were then calculated by analysis of fluorescence data using van’t Hoff plot.
These data indicated that driving force for interaction was mainly hydrophobic in nature and the
process was entropy driven. The information obtained from CD, FT-IR and synchronous fluorescence
spectroscopies revealed that both microenvironment and conformation of HSA was changed.
Molecular docking study confirmed the binding mode obtained by experimental data.
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