Investigations of the molecular mechanism of diltiazem binding to human serum albumin in the presence of metal ions, glucose and urea

2021 ◽  
pp. 1-12
Author(s):  
Sara Asadi Farsad ◽  
Hossein Haghaei ◽  
Mina Shaban ◽  
Mostafa Zakariazadeh ◽  
Somaieh Soltani
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Human Serum ◽  
Molecular Mechanism

Early stage aggregation of human serum albumin in the presence of metal ions

2011 ◽  
Vol 49 (3) ◽  
pp. 337-342 ◽  
Author(s):  
Andrea Stirpe ◽  
Manuela Pantusa ◽  
Bruno Rizzuti ◽  
Luigi Sportelli ◽  
Rosa Bartucci ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Human Serum ◽  
Early Stage

Molecular mechanism of tobramycin with human serum albumin for probing binding interactions: multi-spectroscopic and computational approaches

2017 ◽  
Vol 41 (16) ◽  
pp. 8203-8213 ◽  
Author(s):  
Muslim Raza ◽  
Yun Wei ◽  
Yang Jiang ◽  
Aftab Ahmad ◽  
Saleem Raza ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Molecular Mechanism ◽  
In Silico ◽  
The Novel ◽  
Binding Interactions ◽  
Computational Approaches

Highlighting novelty: comprehensive in vitro and in silico insights for understanding the novel binding site of TOB with HSA.

scholarly journals Pb2+, Cu2+, Zn2+, Mg2+ and Mn2+ reduce the affinities of flavone, genistein and kaempferol for human serum albumin in vitro

2011 ◽  
Vol 63 (3) ◽  
pp. 623-634 ◽  
Author(s):  
Fan Yang ◽  
Jie Wang ◽  
Chunxi Liu ◽  
Xu Xiaochen ◽  
Li Wenjun ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Human Serum ◽  
Blue Shift ◽  
Red Shift ◽  
Presence And Absence

Flavone (Fl), genistein (Gen) and kaempferol (Kol) were studied for their affinities towards human serum albumin (HSA) in the presence and absence of Pb2+,Cu2+,Zn2+,Mg2+ and Mn2+. The fluorescence intensities of HSA decreased with increasing concentration of the three flavonoids. Kaempferol resulted in a blue-shift of the ?em of HSA from 336 to 330 nm; flavone showed an obvious red-shift of the ?em of HSA from 336 to 342 nm; genistein did not cause an obvious blue-shift or red-shift of the ?em of HSA. However, the extents of ?em-shifts induced by the flavonoids in the presence of metal ions were much bigger than that in the absence of mental ions. Pb2+,Cu2+,Zn2+,Mg2+ and Mn2+ reduced the quenching constants of the flavonoids for HSA by 14.6% to 60.7% , 28% to 67.9%,3.5% to 59.4%, 23.2% to 63.7% and 14% to 65%, respectively. The affinities of flavone, genistein and kaempferol for HSA decreased about 10.84%, 10.05%and 3.56% in the presence of Pb2+, respectively. Cu2+ decreased the affinities of flavone, genistein and kaempferol for HSA about 14.04%, 5.14%and 8.89%, respectively. Zn2+ decreased the affinities of flavone, genistein and kaempferol for HSA about 3.79%, 0.55% and 3.58%, respectively. Mg2+ decreased the affinities of flavone, genistein and kaempferol for HSA about 16.94%, 2.94%and 7.04%, respectively. Mn2+ decreased the affinities of flavone, genistein and kaempferol for HSA about 14.24%, 3.66% and 4.78%, respectively.

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