Spectroscopic studies on the drug–drug interaction: the influence of fluoroquinolones on the affinity of tigecycline to human serum albumin and identification of the binding site

Stojanović, Stefan; Nićiforović, Jovan; Živanović, Sandra; Odović, Jadranka; Jelić, Ratomir

doi:10.1007/s00706-020-02627-0

Cited by 17 publications

(9 citation statements)

References 44 publications

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“…For complex 2 , the binding constant increased when ibuprofen was added to the system. Such an increase has been reported before and can be explained by conformational changes in the protein structure caused by non‐competitive binding of two different ligands [57,58] …”

Section: Resultssupporting

confidence: 69%

Spectroscopic and Molecular Docking Study of the Interaction between Neutral Re(I) Tetrazolate Complexes and Bovine Serum Albumin

Łaźniewska

Agostino

Hickey

et al. 2021

Chemistry A European J

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Re(I) complexes have potential in biomedical sciences as imaging agents, diagnostics and therapeutics. Thus, it is crucial to understand how Re(I) complexes interact with carrier proteins, like serum albumins. Here, two neutral Re(I) complexes were used (fac‐[Re(CO)3(1,10‐phenanthroline)L], in which L is either 4‐cyanophenyltetrazolate (1) or 4‐methoxycarbonylphenyltetrazole ester (2), to study the interactions with bovine serum albumin (BSA). Spectroscopic measurements, calculations of thermodynamic and Förster resonance energy transfer parameters, as well as molecular modelling, were performed to study differential binding between BSA and complex 1 and 2. Induced‐fit docking combined with quantum‐polarised ligand docking were employed in what is believed to be a first for a Re(I) complex as a ligand for BSA. Our findings provide a basis for other molecular interaction studies and suggest that subtle functional group alterations at the terminal region of the Re(I) complex have a significant impact on the ability of this class of compounds to interact with BSA.

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Section: Resultssupporting

confidence: 69%

Spectroscopic and Molecular Docking Study of the Interaction between Neutral Re(I) Tetrazolate Complexes and Bovine Serum Albumin

Łaźniewska

Agostino

Hickey

et al. 2021

Chemistry A European J

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“…There is an option that the two drugs can bind independently to different sites in the HSA molecule and there are no changes in the binding affinity of the drug to HSA (independent binding). As already reported, the primary binding site of CAF and FLAVs (QUE, CAT and DIO) is located in site I (subdomain IIA) [ 28 , 29 , 30 , 31 ] as well as TGC [ 24 ]. Therefore, competitive interference is expected between TGC and CAF/FLAVs (QUE, CAT and DIO) accompanied by a decrease in binding affinity of TGC to HSA in the presence of competing for drug (CAF/FLAVs (QUE, CAT and DIO)).…”

Section: Resultsmentioning

confidence: 98%

“…UV–Vis absorption spectroscopy is a convenient and effective method for the steady-state study of protein-drug interactions and complex formation [ 21 ]. All observed changes (hypochromic/hyperchromic effect and/or red/blue shift) in UV-Vis spectra during titration may provide evidence of the existing interaction mode between drugs and HSA [ 22 , 23 , 24 ].…”

Section: Resultsmentioning

confidence: 99%

“…In this work, the effect of CAF and FLAVs (QUE, CAT and DIO) on the binding of TGC to HSA was investigated. In our previous work, it was concluded that Sudlow’s site I, located in subdomain IIA of HSA, was the primary binding site of TGC [ 24 ]. It was published that the primary binding site of CAF and FLAVs (QUE, CAT and DIO) was located in the same binding site [ 28 , 29 , 30 , 31 ], indicating that CAF and FLAVs share the same binding sites in the HSA with TGC.…”

Section: Resultsmentioning

confidence: 99%

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Effect of Caffeine and Flavonoids on the Binding of Tigecycline to Human Serum Albumin: A Spectroscopic Study and Molecular Docking

et al. 2022

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Human serum albumin (HSA) has a very significant role in the transport of drugs, in their pharmacokinetic and pharmacodynamic properties, as well as the unbound concentration of drugs in circulating plasma. The aim of this study was to look into the competition between tigecycline (TGC) and alkaloid (ALK) (caffeine (CAF)), and flavonoids (FLAVs) (catechin (CAT), quercetin (QUE), and diosmin (DIO)) in binding to HSA in simulated physiological conditions using multiple spectroscopic measurements and docking simulations. Fluorescence analysis was used to find the binding and quenching properties of double HSA-TGC and triple HSA-TGC-CAF/FLAV systems. The conformational change of the HSA was analyzed using synchronous fluorescence spectroscopy, Fourier transform infrared spectroscopy, and circular dichroism. Obtained results of spectroscopic analyses indicate that triple complexes of HSA-TGC-CAF/FLAVs are formed without problems and have higher binding affinities than double HSA-TGC. In addition, TGC does not change the microenvironments around the tryptophan (Trp) and tyrosine (Tyr) residues in the presence of ALK and FLAVs. Ultimately, the binding affinity, competition, and interaction nature were explored by docking modeling. Computational outcomes are in good accordance with experimentally obtained results. Accordingly, concluding remarks may be very useful for potential interactions between common food components and drugs.

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“…For resisting viruses the immune response is very important and immune system mediators play a significant role (Calder et al, 2020). Hydrophobic binding, shown through the effect of lipophilicity, is the result of water molecules interacting after they leave the nonpolar surface (Stojanović et al, 2020). Mathematical analysis was important for optimization and individualization of the methods we used (Rosic et al, 2011).…”

Section: Medicinal Effects Of Selected Plant Speciesmentioning

confidence: 99%

Increased Demands for Natural Immuno- Boosters in Selected Tourism Areas

Luković

Banja²,

Nićiforović

2021

Tourism Challenges Amid Covid-19

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Rural areas have been facing distinctive challenges during the COVID-19 pandemic. As in other parts of the world, in the Republic of Serbia noticed movement of people from places with high concentration of settlements, like cities, into less densely populated communities. Searching for rural, natural, wild areas far away from cities, tourists made different pressures on local environment (sound, litter, pressure on natural resources, pollution) but also increased demands for healthier way of living in accordance with World Health Organization recommendation during the Covid 19 period. Besides a clear environment, they would like to enjoy locally produced food and wild edible plants as a source of minerals, vitamins and other functional substances for strengthening immunity. Using standard botanical questionnaire, the research was conducted in selected rural areas with the aim to create a list of the most wanted wild edible plants by tourists and to overview their potential contribution to immune system strengthening in the COVID-19 pandemic period.

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Spectroscopic studies on the drug–drug interaction: the influence of fluoroquinolones on the affinity of tigecycline to human serum albumin and identification of the binding site

Cited by 17 publications

References 44 publications

Spectroscopic and Molecular Docking Study of the Interaction between Neutral Re(I) Tetrazolate Complexes and Bovine Serum Albumin

Spectroscopic and Molecular Docking Study of the Interaction between Neutral Re(I) Tetrazolate Complexes and Bovine Serum Albumin

Effect of Caffeine and Flavonoids on the Binding of Tigecycline to Human Serum Albumin: A Spectroscopic Study and Molecular Docking

Increased Demands for Natural Immuno- Boosters in Selected Tourism Areas

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