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3699424 
Journal Article 
Interaction of Human Serum Albumin and Water Soluble Cationic Pyridyl Corrole Gallium Complex 
Wen Jinyan; Lu Biaobiao; Zhang Yang; Wang Jiamin; Ying Xiao; Wang Hui; Ji Liangnian; Liu Haiyang 
2015 
1 
Gaodeng Xuexiao Huaxue Xuebao / Chemical Journal of Chinese Universities
ISSN: 0251-0790 
36 
6 
1033-1041 
WOS:000359961400001 
The interaction between gallium 5, 10, 15-tris(4-methylpyridiniumyl) corrole (1-Ga) and human serum albumin(HSA) was investigated using UV-Vis spectra, fluorescence spectra, circular dichroism(CD) spectra and molecular docking simulation. The results reveal that the fluorescence quenching of HSA by 1-Ga is a static quenching process. The binding constant of complex 1-Ga with HSA is 2. 82x10(4) L/mol, and binding distance r=3. 342 nm. Thermodynamic parameters show the interaction is mainly driven by hydrophobic and hydrogen binding forces. Site marker competition experiment indicates 1-Ga preferably bind to ibuprofen site 11 of HSA. Also, alpha-helix content Of HSA will decrease upon binding 1-Ga as indicated by UV-Vis and CD spectroscopy. Molecular docking simulation confirmed 1-Ga bind to the hydrophobic pocket site 11 in domain III A of HSA. 
Corrole; Gallium; Human serum albumin; Interaction