Coupling between fatty acid binding and sulfhydryl oxidation in bovine serum albumin

1983 ◽  
Vol 136 (2) ◽  
pp. 291-295 ◽  
Author(s):  
Kenji TAKABAYASHI ◽  
Teruaki IMADA ◽  
Yuji SAITO ◽  
Yuji INADA
Keyword(s):  
Fatty Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Fatty Acid Binding ◽  
Sulfhydryl Oxidation

Bovine serum albumin: characterization of a fatty acid binding site on the N-terminal peptic fragment using a new spin-label

Biochemistry ◽  
1984 ◽  
Vol 23 (25) ◽  
pp. 5930-5932 ◽  
Author(s):  
J. C. Hsia ◽  
L. T. Wong ◽  
C. T. Tan ◽  
S. S. Er ◽  
S. Kharouba ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Spin Label ◽  
Bovine Serum ◽  
Fatty Acid Binding ◽  
Fatty Acid Binding Site

scholarly journals Insight into the Molecular Interaction of Cloxyquin (5-chloro-8-hydroxyquinoline) with Bovine Serum Albumin: Biophysical Analysis and Computational Simulation

2019 ◽  
Vol 21 (1) ◽  
pp. 249 ◽  
Author(s):  
Kamonrat Phopin ◽  
Waralee Ruankham ◽  
Supaluk Prachayasittikul ◽  
Virapong Prachayasittikul ◽  
Tanawut Tantimongcolwat
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Hydrophobic Interaction ◽  
Bovine Serum ◽  
Computational Simulation ◽  
Docking Simulation ◽  
Biophysical Model ◽  
Therapeutic Drug ◽  
Fatty Acid Binding ◽  
Binding Behavior

Cloxyquin is a potential therapeutic compound possessing various bioactivities, especially antibacterial, antifungal, cardioprotective, and pain relief activities. Herein, the interaction mechanism between cloxyquin and bovine serum albumin (BSA) has been elucidated in order to fulfill its pharmacokinetic and pharmacodynamic gaps essential for further development as a therapeutic drug. Multi-spectroscopic and biophysical model analysis suggested that cloxyquin interacts with BSA via a static process by ground-state complex formation. Its binding behavior emerged as a biphasic fashion with a moderate binding constant at the level of 104 M−1. Thermodynamic analysis and molecular docking simulation concurrently revealed that hydrophobic interaction is a major driving force for BSA–cloxyquin complexation. Binding of cloxyquin tends to slightly enlarge the monomeric size of BSA without a significant increase of aggregate fraction. Cloxyquin preferentially binds into the fatty acid binding site 5 (FA5) of the BSA via hydrophobic interaction amongst its quinoline scaffold and Phe550, Leu531, and Leu574 residues of BSA. The quinoline ring and hydroxyl moiety of cloxyquin also form the π–π interaction and the hydrogen bond with Phe506. Our data indicate a potential function of serum albumin as a carrier of cloxyquin in blood circulation.

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