Fluorometric study of tetracycline-bovine serum albumin interaction

Popov, P.G.; Vaptzarova, K. I.; Kossekova, Ganka P.; Николов, Тодор

doi:10.1016/0006-2952(72)90388-7

Cited by 14 publications

(6 citation statements)

References 9 publications

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“…32,33) By way of comparison, DH b ranging from 2 to 3 kcal mol Ϫ1 have been reported for various TC derivatives interacting with BSA. 29) We obtained a somewhat different value for AHTC, but the methods of determination and the experimental conditions may not be directly comparable.…”

Section: Fluorescence Changes Upon Ahtc-bsa Interactionmentioning

confidence: 80%

“…29,30) The fluorescence intensity is enhanced in non-polar environments as a consequence of an increase in the quantum yield, which is accompanied by a spectral shift towards lower wavelengths. 29,30) We found similar polarity sensitivity for AHTC fluorescence. In comparison with the emission in buffer, the spectrum of AHTC in butanol was blue-shifted by 30 nm and the intensity increased about twofold (Fig.…”

Section: Fluorescence Changes Upon Ahtc-bsa Interactionmentioning

confidence: 99%

See 1 more Smart Citation

Binding of the Highly Toxic Tetracycline Derivative, Anhydrotetracycline, to Bovine Serum Albumin

Burgos

Fernández

Celej

et al. 2011

Biological & Pharmaceutical Bulletin

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Tetracycline (TC) derivatives comprise a group of bacteriostatic antibiotics extensively used in human and veterinary medicine and in acquaculture, and as animal growth promoters due to their safe toxicological profile.1) More recently, they have been proposed as anti-amyloidogenic drugs since they can interfere with protein conformational changes and self-assemblies associated with protein misfolding and deposition diseases. 2-4)Despite their popular use, TC derivatives are highly unstable and some degradation products formed during the storage or normal use of the drugs are pharmacologically toxic or inactive compounds.5) Anhydrotetracycline (AHTC) is one of the major degradation products of TC that has been linked to several side effects of the drug, e.g., cutaneous phototoxicity 6) and Fanconi-type syndrome. 7) AHTC has also proven to be more toxic than TC against environmentally relevant bacteria. 8)AHTC can be produced by dehydration in acid media, 5,8) by photolysis in mild reducing conditions 6,9,10) or during high-temperature treatments.11) Removal of a water molecule from the C5a-C6 positions of TC by treatment with warm mineral acid gives the anhydroderivative (Fig. 1).12) Dehydration leads to significant changes in aromatization and planarity of the tetracyclic moiety, 13,14) showing variations in potency, 15) mechanism of action 1) and lipophilicity 16,17) as compared to the parent compound. Changes in chemical configuration can also modulate the interaction of drugs with serum proteins. 18)Serum albumins are the main carriers of physiological metabolites and pharmacological drugs in blood. Protein binding has a significant impact on the pharmacokinetics and biological activity of drugs and modulates the toxicity of bound substances, attenuates adverse reactions and prolongs the in vivo half-life of therapeutic agents. 18-21)The facts outlined above prompted us to investigate the interaction of AHTC with bovine serum albumin (BSA) using three biophysical techniques. Binding affinity and number of interacting ligands were assessed by fluorimetric titration. . Drug binding was enthalpically and entropically driven and seemed to involve hydrophobic interactions. AHTC fluorescence enhancement and hypsochromic shifts observed upon binding suggested a low-polarity location excluded from water for the bound drug. Our data are useful for evaluating the biodisponibility of the pharmacophore and the dynamic distribution of the toxic derivative.

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Section: Fluorescence Changes Upon Ahtc-bsa Interactionmentioning

confidence: 80%

Section: Fluorescence Changes Upon Ahtc-bsa Interactionmentioning

confidence: 99%

Binding of the Highly Toxic Tetracycline Derivative, Anhydrotetracycline, to Bovine Serum Albumin

Burgos

Fernández

Celej

et al. 2011

Biological & Pharmaceutical Bulletin

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“…At physiological pH, doxycycline is partly in anionic form. Thermodynamic and fluorometric studies demonstrated that the interaction of doxycycline with the negatively charged albumin is hydrophobic (Popov et al, 1972). It should be noted that albumin may not be the only plasma protein involved in serum doxycycline binding.…”

Section: Discussionmentioning

confidence: 98%

Doxycycline binding to plasma albumin of several species

Riond

Riviere

1989

Vet Pharm & Therapeutics

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The affinity of doxycycline for crystalline plasma albumin fraction V, originating from sheep, dogs, cats, cows, pigs and humans, was evaluated by means of double-reciprocal and Scatchard plots. Mathematical modelling and weighted least-squares non-linear regression analysis of each Scatchard plot identified one binding component characterized by one high affinity binding site, and a second component attributed to non-specific binding to albumin. Association constants for this binding site ranged from 38,471 +/- 13,369 (SEM) l/mol for the interaction of doxycycline with ovine albumin to 6405 +/- 2375 l/mol for the interaction of doxycycline with human albumin. Statistical evaluation of the results suggested slight species-related differences in the values of association constants. Diphenylhydantoin, phenobarbital or carbamazepine did not displace doxycycline from binding sites on bovine albumin.

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“…The effect of OTC contamination on human health has aroused worldwide attention and research on the toxicity of OTC at the whole organism level (10)(11)(12), organ level (13), and cellular level (14). The interaction between OTC and serum albumin at the molecular level by using spectroscopic methods (15)(16)(17)(18) has also been studied, but the inner filter effect was not considered. For the BSA-OTC system, the inner filter effect is caused by the absorption of the excitation and emission wavelengths by OTC and BSA in fluorescence experiments, which change the intensity of fluorescence spectra of BSA, affecting the binding parameters calculated from the fluorescence data.…”

Section: Introductionmentioning

confidence: 99%

Binding of Oxytetracycline to Bovine Serum Albumin: Spectroscopic and Molecular Modeling Investigations

Chi

Liu

Teng

et al. 2010

J. Agric. Food Chem.

210

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The residue of the widely used veterinary drug oxytetracycline (OTC) in the environment (e.g., animal food, soils, surface water, and groundwater) is potentially harmful. Knowledge of its binding to proteins contributes to the understanding of its toxicity in vivo. This work establishes the binding mode of OTC with bovine serum albumin (BSA) under physiological conditions by spectroscopic methods and molecular modeling techniques. The inner filter effect was eliminated to get accurate data (binding parameters). On the basis of the thermodynamic results and site marker competition experiments, it was considered that OTC binds to site II (subdomain IIIA) of BSA mainly by electrostatic interaction. Furthermore, using the BSA model established with CPHmodels, molecular docking and some other molecular modeling methods were applied to further define that OTC interacts with the Arg 433, Arg 436, Ala 429, and Pro 516 residues of BSA. In addition, UV-visible absorption, synchronous fluorescence, and circular dichroism (CD) results showed that the binding of OTC can cause conformational and some microenvironmental changes of BSA. The work provides accurate and full basic data for clarifying the binding mechanisms of OTC with BSA in vivo and is helpful for understanding its effect on protein function during its transportation and distribution in blood.

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Fluorometric study of tetracycline-bovine serum albumin interaction

Cited by 14 publications

References 9 publications

Binding of the Highly Toxic Tetracycline Derivative, Anhydrotetracycline, to Bovine Serum Albumin

Binding of the Highly Toxic Tetracycline Derivative, Anhydrotetracycline, to Bovine Serum Albumin

Doxycycline binding to plasma albumin of several species

Binding of Oxytetracycline to Bovine Serum Albumin: Spectroscopic and Molecular Modeling Investigations

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