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

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.

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In Silico Prediction of Interactions between Site II on Human Serum Albumin and Profen Drugs

ISRN Pharmaceutics ◽

10.1155/2013/818364 ◽

2013 ◽

Vol 2013 ◽

pp. 1-8 ◽

Cited By ~ 2

Author(s):

Hideto Isogai ◽

Noriaki Hirayama

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Binding Sites ◽

Binding Mode ◽

X Ray ◽

Docking Simulations ◽

X Ray Crystallography ◽

Inflammatory Drugs ◽

Multiple Template

Since binding of a drug molecule to human serum albumin (HSA) significantly affects the pharmacokinetics of the drug, it is highly desirable to predict the binding affinity of the drug. Profen drugs are a widely used class of nonsteroidal anti-inflammatory drugs and it has been reported that several members of the profen class specifically bind to one of the main binding sites named site II. The actual binding mode of only ibuprofen has been directly confirmed by X-ray crystallography. Therefore, it is of interest whether other profen drugs are site II binders. Docking simulations using multiple template structures of HSA from three crystal structures of complexes between drugs and HSA have demonstrated that most of the currently available profen drugs should be site II binders.

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Interaction of the Fungicide Tebuconazole with Human Serum Albumin: A Preliminary Study

Folia Veterinaria ◽

10.2478/fv-2018-0020 ◽

2018 ◽

Vol 62 (2) ◽

pp. 85-91 ◽

Cited By ~ 1

Author(s):

J. Staničová ◽

K. Želonková ◽

V. Verebová ◽

B. Holečková ◽

J. Dianovský

Keyword(s):

Secondary Structure ◽

Human Serum Albumin ◽

Fluorescence Quenching ◽

Serum Albumin ◽

Human Serum ◽

Binding Sites ◽

Triazole Fungicides ◽

Number Of Binding Sites ◽

Preliminary Study ◽

Protein Macromolecule

Abstract The interactions between the fungicide tebuconazole and human serum albumin were investigated using fluorescence and circular dichroism spectroscopies. The experimental results showed that the fluorescence quenching of the protein by the tebuconazole molecule was a result of the formation of a ligand-protein complex with a binding constant of 8.51×103 l.mol−1 and the number of binding sites in the macromolecule was close to 1. These findings demonstrated the fact that although the binding affinity of tebuconazole to the protein may be slight, it was very similar to other triazole fungicides. In addition, tebuconazole stabilized the α-helical secondary structure of the human serum albumin due to the increase of the α-content in the protein macromolecule.

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Molecular mechanistic vision on binding interaction of triptan drug, a serotonin (5-HT1) agonist with human serum albumin through multispectral and computational assessments

European Journal of Chemistry ◽

10.5155/eurjchem.11.2.145-155.1971 ◽

2020 ◽

Vol 11 (2) ◽

pp. 145-155

Author(s):

Manjushree Makegowda ◽

Revanasiddappa Hosakere Doddarevanna

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Clinical Medicine ◽

Fluorescence Emission ◽

Binding Constants ◽

Binding Interaction ◽

Binding Ability ◽

Ft Ir ◽

Ft Ir Spectroscopy

The triptan drug such as eletriptan in combination with hydrochloride (ETP) is a 5-HT1 receptor agonist used to treat the migraine headache. Human serum albumin (HSA), the fundamental serum protein, executes various functions, that includes transporting and binding of many ligands. HSA binding interaction with ETP is elucidated from molecular docking in composite with fluorescence (emission, 3D and synchronous), UV-vis and FT-IR spectroscopy at 296, 304 and 312 K (pH = 7.40). ETP after interaction modified the HSA secondary structure and its micro-environments. Energy transfer and thermodynamic parameters were evaluated. Various quenching and binding constants were computed for formed ETP-HSA complex. The dominant interactive forces for ETP and HSA binding are hydrogen bonds join up with van der Waals extent possibly at site III (IB). The presence of Ca2+, Co2+, Na+, Mg2+ and Fe3+ ions significantly affected binding ability of ETP towards HSA. The essentialness of this investigation is beneficial in life sciences, medicinal chemistry, pharmaceutical industry and clinical medicine.

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

Journal of Molecular Structure ◽

10.1016/j.molstruc.2009.04.018 ◽

2009 ◽

Vol 929 (1-3) ◽

pp. 159-166 ◽

Cited By ~ 56

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

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Synthesis of 2-aminonaphthalene-1-sulfonic acid Schiff bases and their interactions with human serum albumin

Turkish Journal of Biochemistry ◽

10.1515/tjb-2019-0284 ◽

2020 ◽

Vol 0 (0) ◽

Author(s):

Huiqing Li ◽

Qiang Gao

Keyword(s):

Schiff Base ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Electrostatic Interactions ◽

Interaction Mechanism ◽

Protein Secondary Structure ◽

Binding Constants ◽

Resonance Light Scattering ◽

Binding Model

AbstractObjectivesHuman serum albumin (HSA) can bind and transport many substances to cells to meet various needs of the organism. The binding efficacy of HSA to these substances directly affects their functions. In this paper two Schiff base compounds were synthesized to explore the interaction between HSA and both compounds.MethodsFluorescence spectra and an AutoDock model were utilized to investigate the interaction mechanism and binding model between proteins and Schiff base products. The conformation change of HSA was detected by resonance light scattering and circular dichroism spectra.ResultsThe two compounds bound easily with HSA, with binding constants of 104. The binding sites for both compounds in HSA were within an appropriate distance for long-range interactions. Both compounds are accommodated in hydrophobic domains of HSA. However, electrostatic interactions and other supermolecular forces coexist between the compounds and protein. Binding of these compounds disturbed the protein secondary structure and caused a certain degree of destabilization.ConclusionsThe two Schiff base compounds can interact with HSA with high efficacy, which is helpful for explore the application of this type of Schiff base in biomedical research.

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