Chloramphenicol binding to human serum albumin: Determination of binding constants and binding sites by steady-state fluorescence

2009 ◽  
Vol 929 (1-3) ◽  
pp. 159-166 ◽  
Author(s):  
Fei Ding ◽  
Guangyu Zhao ◽  
Shoucong Chen ◽  
Feng Liu ◽  
Ying Sun ◽  
...  
Keyword(s):  
Steady State ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Binding Constants ◽  
Steady State Fluorescence

scholarly journals N-bromosuccinimide-oxidized human serum albumin as a tool for the determination of drug binding sites of human serum albumin.

1983 ◽  
Vol 31 (3) ◽  
pp. 971-978 ◽  
Author(s):  
HIROKO SAKAMOTO ◽  
IZUMI NAGATA ◽  
KIYOMI KIKUCHI ◽  
MASAKO AIDA ◽  
MASACHIKA IRIE
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Drug Binding ◽  
Drug Binding Sites

Spectroscopic and thermodynamic determination of three distinct binding sites for Co(II) ions in human serum albumin☆

2009 ◽  
Vol 103 (7) ◽  
pp. 1005-1013 ◽  
Author(s):  
Magdalena Sokołowska ◽  
Małgorzata Wszelaka-Rylik ◽  
Jarosław Poznański ◽  
Wojciech Bal
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Thermodynamic Determination

scholarly journals The Effect of Tigecycline on the Binding of Fluoroquinolones to Human Serum Albumin

2018 ◽  
Vol 19 (1) ◽  
pp. 17-25 ◽  
Author(s):  
Ratomir M. Jelic ◽  
Stefan D. Stojanovic ◽  
Jelena D. Beric ◽  
Jadranka Odovic
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Interaction Mechanism ◽  
Binding Constants ◽  
Binding Mode ◽  
Binding Ability ◽  
Free Plasma

AbstractThe co-administration of several drugs in multidrug therapy may alter the binding of each drug to human serum albumin (HSA) and, thus, their pharmacology effect. Therefore, in this study, the interaction mechanism between HSA and two fluoroquinolones (FQs), sparfloxacin (SPF) and levofloxacin (LVF), was investigated using fluorescence and absorption methods in the absence and presence of the competing drugtigecycline (TGC). The the UV-Vis and fluorescence spectroscopy results showed that the fluorescence quenching of HSA was a result of the formation of the HSA-SPF and HSA-LVF complexes. The fluorescence quenching of HSA-TGC revealed that tigecycline can regulate the binding sites, binding mode and binding affinity of fluoroquinolones. The binding constants (KA) and binding sites (n) of the interaction systems were calculated. The results confirmed that the KA values of the HSA-FQ system decreased in the presence of TGC, indicating that TGC can affect the binding ability of FQ for HSA. This interaction may increase the free plasma concentration of unbound FQ and enhance their pharmacology effect.

Determination of the binding constants of nanomarkers of the fluorescein family to human serum albumin

2012 ◽  
Vol 67 (2) ◽  
pp. 208-212 ◽  
Author(s):  
I. M. Vlasova ◽  
Ju. A. Gordeeva ◽  
A. A. Vlasov ◽  
A. M. Saletsky
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Constants
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