Voltammetric and spectroscopic studies on the interaction of tilmicosin with bovine serum albumin at different pHs

Bíçer, Ender; Özdemír, Serkan

doi:10.1016/j.jelechem.2011.04.001

Cited by 8 publications

(8 citation statements)

References 46 publications

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“…Tilmicosin is the semisynthetic derivative of tylosin ( Figure 1), which has a similar antibacterial spectrum to tylosin [3]. Furthermore, tilmicosin has a better antibiosis effect than tylosin against gram-negative organisms, mycoplasma, pasteurella, and can be used to control mycoplasma avian disease and mastitis of lactating cows [4][5][6]. Due to effective antibiotic properties, tylosin and tilmicosin are widely applied to treat bacterial infection in various animals, including beef cattle swine and poultry [4,7].…”

Section: Introductionmentioning

confidence: 99%

“…Tylosin and tilmicosin have a low metabolic rate after administration, and their residues are widely distributed in the body fluids and tissues of livestock [7,10]. In addition, it was reported that tylosin and tilmicosin residues and can be used to control mycoplasma avian disease and mastitis of lactating cows [4][5][6]. Due to effective antibiotic properties, tylosin and tilmicosin are widely applied to treat bacterial infection in various animals, including beef cattle swine and poultry [4,7].…”

Section: Introductionmentioning

confidence: 99%

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Design of Novel Haptens and Development of Monoclonal Antibody-Based Immunoassays for the Simultaneous Detection of Tylosin and Tilmicosin in Milk and Water Samples

et al. 2019

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In this work, a monoclonal antibody-based indirect competitive enzyme-linked immunosorbent assay (icELISA) was established to detect tylosin and tilmicosin in milk and water samples. A sensitive and specific monoclonal antibody was prepared by rational designed hapten, which was achieved by directly oxidizing the aldehyde group on the side chain of tylosin to the carboxyl group. Under the optimized conditions, the linear range of icELISA for tylosin and tilmicosin were 1.3 to 17.7 ng/mL and 2.0 to 47.4 ng/mL, with half-maximal inhibition concentration (IC50) values of 4.7 and 9.6 ng/mL, respectively. The cross-reactivity with other analogues of icELISA was less than 0.1%. The average recoveries of icELISA for tylosin and tilmicosin ranged from 76.4% to 109.5% in milk and water samples. Besides, the detection results of icELISA showed good correlations with HPLC-MS/MS. The proposed icELISA was satisfied for rapid and specific screening of tylosin and tilmicosin residues in milk and water samples.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Design of Novel Haptens and Development of Monoclonal Antibody-Based Immunoassays for the Simultaneous Detection of Tylosin and Tilmicosin in Milk and Water Samples

et al. 2019

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“…The binding of tilmicosin to bovine serum albumin was reported by electrochemical and UV-vis spectroscopic methods [ 12 ]. Due to several questions remained opened, in this study the interaction of tilmicosin (TIL) with bovine serum albumin (BSA) was investigated using optical spectroscopic (UV-vis, Photoluminescence) and Differential Scanning Calorimetric (DSC) methods.…”

Section: Introductionmentioning

confidence: 99%

Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin

et al. 2018

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Tilmicosin is a widely used antibiotic in veterinary applications. Its antimicrobial activity is ranged from Gram-positive and some Gram-negative bacteria towards activities against Mycoplasma and Chlamydia. Adsorption affinity of tilmicosin antibiotics towards bovine serum albumin was investigated by both spectroscopic (UV-vis, Photoluminescence) and calorimetric methods. The interaction was determined on the basis of quenching of albumin by tilmicosin. Results confirm noncovalent binding of tilmicosin on bovine serum albumin with 1:1 stoichiometry associated with pK = 4.5, highlighting possible removal of tilmicosin molecules from the albumin surface through exchange reactions by known competitor molecules. Calorimetric measurements have confirmed the weak interaction between tilmicosin and albumin and reflect enhanced denaturation of the albumin in the presence of tilmicosin antibiotic. This process is associated with the decreased activation energy of conformational transition of the albumin. It opens a new, very quick reaction pathway without any significant effect on the product by noncovalent binding the tilmicosin molecules to the protein molecules. Results highlight the medical importance of these investigations by considerable docking of the selected antibiotic molecules on serum albumins. Although the binding may cause toxic effects in living bodies, the strength of the binding is weak enough to find competitor molecules for effective removals from their surface.

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“…26 Some techniques such as gel electrophoresis, 42 X-ray crystallography, 43 NMR, 44 fluorescence, 45,46 differential scanning calorimetry (DSC), 47 infrared spectroscopy, 37,40 UV/Vis. spectroscopy, [46][47][48] circular dichroism (CD) spectroscopy 49 and electrochemistry, [50][51][52] have been intensively used to study the molecular interactions. In recent years, there has been a growing interest in the electrochemical and spectroscopic investigation of molecular interations.…”

Section: Introductionmentioning

confidence: 99%

“…In recent years, there has been a growing interest in the electrochemical and spectroscopic investigation of molecular interations. 51,52 Also, spectroscopic and voltammetric techniques have been testified to be of high sensitivity, relatively low cost, direct monitoring and simplicity. [46][47][48][49][53][54][55][56][57] Except for only the interaction of albumin and fusidic acid by zone microelectrophoresis in 0.05 M barbitone sodium buffer pH 8.4, 58 the voltammetric and spectroscopic studies on the interactions of three steroids which are presented in Scheme 1 ( fusidic acid (FA), ouabain (OUB) and ethynodioldiacetate (ETH), respectively) with HSA at the physiological pH could not be traced in the literature.…”

Section: Introductionmentioning

confidence: 99%

Temperature Effect on Binding Affinity and Stoichiometry Between Some Steroids and Human Serum Albumin

Özdemír

Bíçer

2016

J. Chil. Chem. Soc.

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The temperature dependence of the interactions between some steroids (fusidic acid, ouabain and ethynodioldiacetate) and human serum albumin (HSA) at physiological pH (7.4) were studied systematically by square-wave voltammetry. Also, these interactions were proven by means of UV-Vis. absorption spectroscopy and FT-IR spectroscopy techniques. The interaction parameters (binding constants and stoichiometries) at temperature range of 297.5-312.5 K were determined from electrochemical data. It is worthy that the temperature has played a positive role on the interactions of fusidic acid with HSA; however it has negative effective on the interaction parameters of HSA with ouabain or ethynodioldiacetate.

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Voltammetric and spectroscopic studies on the interaction of tilmicosin with bovine serum albumin at different pHs

Cited by 8 publications

References 46 publications

Design of Novel Haptens and Development of Monoclonal Antibody-Based Immunoassays for the Simultaneous Detection of Tylosin and Tilmicosin in Milk and Water Samples

Design of Novel Haptens and Development of Monoclonal Antibody-Based Immunoassays for the Simultaneous Detection of Tylosin and Tilmicosin in Milk and Water Samples

Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin

Temperature Effect on Binding Affinity and Stoichiometry Between Some Steroids and Human Serum Albumin

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