Application of Azure C for the extractive spectrophotometric determination of microgram amounts of penicillin

Gowda, A.Thimme; Gowda, N. M. Made; Gowda, H. Sanke; Rancappa, K.S

doi:10.1016/0160-5402(85)90028-2

Cited by 11 publications

(5 citation statements)

References 7 publications

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“…Azure C is an important photosensitizing dye; it can actively induce photoactivated dye toxicity in a DNA nicking assay and the targeted neuronal lesion . This water‐soluble thiazine dye also has been used for the extractive spectrophotometric determination of microgram amounts of penicillin . Serum albumins have also attracted enormous research interest as a prime molecular target .…”

Section: Introductionmentioning

confidence: 99%

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Molecular binding of toxic phenothiazinium derivatives, azures to bovine serum albumin: A comparative spectroscopic, calorimetric, and in silico study

Das

Islam

Jana

et al. 2017

J of Molecular Recognition

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In this paper, the comparative binding behavior of antimalarial drug azure A, azure B and azure C with bovine serum albumin (BSA) has been studied. The interaction has been confirmed by multispectroscopic (UV, fluorescence, Fourier transform infrared (FT-IR), and circular dichroism) and molecular docking techniques. The experimental results show that azure B has the highest BSA binding affinity followed by azure A and azure C. The experimental evidence of binding showed a static quenching mechanism in the interaction azures with BSA. The isothermal titration calorimetry result reveals that the binding was exothermic with positive entropy contribution in each case. The thermodynamic parameters ΔH, ΔG, and ΔS at 25°C were calculated, which indicates that the weak van der Waals forces and hydrogen bonding rather than the hydrophobic effect played an important role in the interaction. According to the theory of Förster nonradiative energy transfer, the distance (r) between the donor (BSA) and acceptor azures found to be <7 nm in all the case. The circular dichroism and FT-IR studies show that the content of α-helix structure has increased for the azures-BSA system. Overall, experimental studies characterize the interaction dynamics and energetics of the binding of three toxic analogs towards the physiologically relevant serum albumins. We hope, the outcome of this work will be most helpful for synthesizing a new type of phenothiazinium derivatives of the better therapeutic application.

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Section: Introductionmentioning

confidence: 99%

“…10 This water-soluble thiazine dye also has been used for the extractive spectrophotometric determination of microgram amounts of penicillin. 11 Serum albumins have also attracted enormous research interest as a prime molecular target. [12][13][14] Bovine serum albumin (BSA) is a globular heart-shaped protein, with 583 amino acid residue monomers of 66.4 kDa.…”

mentioning

confidence: 99%

Molecular binding of toxic phenothiazinium derivatives, azures to bovine serum albumin: A comparative spectroscopic, calorimetric, and in silico study

Das

Islam

Jana

et al. 2017

J of Molecular Recognition

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“…In the pharmaceutical industry, they are used as psychotherapeutic, antiemetic, and antihistamine drugs ~1-3), while some are employed as chromogens in the spectrophotometric determination of transition metals in solutioff [4][5][6]. In the pharmaceutical industry, they are used as psychotherapeutic, antiemetic, and antihistamine drugs ~1-3), while some are employed as chromogens in the spectrophotometric determination of transition metals in solutioff [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Synthesis and characterization of iridium chloride complexes: I. Use of N-alkylphenothiazine drugs as ligands

Gowda

Kyi

Zhang

1993

Transition Met Chem

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Iridium complexes of N-alkylphenothiazines have been prepared in MeOH. The polynuclear complexes obtained have been characterized by elemental analyses, magnetic susceptibilities, molar conductivities, thermogravimetric analysis and spectral data. The molecular formulae of the new complexes are as follows: [Ir3(LH)4Cllo]C1 z'xMeOH, where L = chlorpromazine (CP), promethazine (PM) or ethopropazine (EP), and x = 1 for CP and 2 for PM or EP; [Ir(TFH2)2C14] [IrC161" MeOH, where TF = trifluoperazine; and [Ir3(TRH)2C1 ll(MeOH)]CI'MeOH and [Ir4(TRH)3ClIs], where TR=thioridazine. The complexes are diamagnetic in nature. Tentative structures are proposed for the complexes.

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“…The planktonic culture was removed from 36 wells for each strain, and the biofilms were washed with phosphatebuffered saline (PBS) prior to addition of penicillin solution (200 l containing 8.3 g/ml per well, corresponding to 100 g/ml per 12 wells). This concentration is within the linear range for penicillin determination by the azure C assay (14,27). The plates were incubated (room temperature, 1 h) prior to removal and pooling of the supernatants from each set of 12 wells.…”

Section: Vol 51 2007 Rapa Confers Antibiotic Resistance To E Coli mentioning

confidence: 99%

Role of the rapA Gene in Controlling Antibiotic Resistance of Escherichia coli Biofilms

Lynch

Dixon

Benoit

et al. 2007

Antimicrob Agents Chemother

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By using a high-throughput screening method, a mutant of a uropathogenic Escherichia coli strain affected in the rapA gene was isolated. The mutant formed normal-architecture biofilms but showed decreased penicillin G resistance, although the mutation did not affect planktonic cell resistance. Transcriptome analysis showed that 22 genes were down-regulated in the mutant biofilm. One of these genes was yhcQ, which encodes a putative multidrug resistance pump. Mutants with mutations in this gene also formed biofilms with decreased resistance, although the effect was less pronounced than that of the rapA mutation. Thus, an additional mechanism(s) controlled by a rapA-regulated gene(s) was involved in wild-type biofilm resistance. The search for this mechanism was guided by the fact that another down-regulated gene in rapA biofilms, yeeZ, is suspected to be involved in extra cell wall-related functions. A comparison of the biofilm matrix of the wild-type and rapA strains revealed decreased polysaccharide quantities and coverage in the mutant biofilms. Furthermore, the (fluorescent) functional penicillin G homologue Bocillin FL penetrated the mutant biofilms more readily. The results strongly suggest a dual mechanism for the wild-type biofilm penicillin G resistance, retarded penetration, and effective efflux. The results of studies with an E. coli K-12 strain pointed to the same conclusion. Since efflux and penetration can be general resistance mechanisms, tests were conducted with other antibiotics. The rapA biofilm was also more sensitive to norfloxacin, chloramphenicol, and gentamicin.Bacterial biofilms are differentiated communities of sessile cells. Infections involving biofilms play a major role in such diverse medical conditions as endocarditis (24), cystic fibrosis (29), otitis media (17), and urinary tract infections (3), presenting a significant threat to human health (12, 16). Although this sessile mode of growth has long been known, the fact that it constitutes a normal part of the bacterial life cycle has been recognized only relatively recently. The medical importance of biofilms lies in the fact that in comparison to their free-living (planktonic) counterparts, biofilms possess increased resistance to antimicrobial agents (12, 16), and consequently, diseases in which biofilms have a dominant role tend to be chronic and difficult to eradicate.The focus of this study was uropathogenic Escherichia coli (UPEC), which is primarily responsible for urinary tract infections. These affect almost 1 billion women each year. UPEC biofilms can form on the epithelium of the bladder and upper urinary tract (28), as well as intracellularly, evading host defenses (1, 2) and resulting in a disease that is often chronic.Several genes play a role in biofilm formation (9,11,20), but whether the same genes are involved in the development of biofilm resistance has been relatively little studied. Mah et al. (21) identified nvdB gene mutants whose antibiotic resistance was not affected while they were in the planktonic stat...

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Application of Azure C for the extractive spectrophotometric determination of microgram amounts of penicillin

Cited by 11 publications

References 7 publications

Molecular binding of toxic phenothiazinium derivatives, azures to bovine serum albumin: A comparative spectroscopic, calorimetric, and in silico study

Molecular binding of toxic phenothiazinium derivatives, azures to bovine serum albumin: A comparative spectroscopic, calorimetric, and in silico study

Synthesis and characterization of iridium chloride complexes: I. Use of N-alkylphenothiazine drugs as ligands

Role of the rapA Gene in Controlling Antibiotic Resistance of Escherichia coli Biofilms

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