Spectroscopic Studies on the Interaction of Acid Yellow With Bovine Serum Albumin

Pan, Xingren; Liu, Rutao; Qin, Pengfei; Wang, Li; Zhao, Xingchen

doi:10.1016/j.jlumin.2009.11.004

Cited by 102 publications

(53 citation statements)

References 38 publications

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“…The binding of toxins to serum albumins may have physiological effects, because they control their free, active concentrations and affect the duration and intensity of their effects. The free concentration available for toxic action can be effectively reduced by high binding to proteins (Pan, Liu, Qin, Wang, & Zhao, 2010). There is evidence of conformation changes of bovine serum albumin (BSA) induced by its interaction with low molecular weight dye and drugs, which appears to affect the secondary and tertiary structure of albumin (Hushcha, Luik, & Naboka, 2000;kamat, 2005).…”

Section: Introductionmentioning

confidence: 99%

Study on the interaction of food colourant quinoline yellow with bovine serum albumin by spectroscopic techniques

2012

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Section: Introductionmentioning

confidence: 99%

Study on the interaction of food colourant quinoline yellow with bovine serum albumin by spectroscopic techniques

2012

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“…Phenylalanine is not much sensitive as compare to the Trp and Tyr, therefore the quantum yield of this residue is rather low as compare to other residues [28], therefore the emission from this residue can be ignored. The synchronous fluorescence spectra with Δλ=20 and 60 nm are characteristics of Tyr and Trp residues, respectively [31].…”

Section: Binding Parameters Of Bsa With Cationic Amphiphilesmentioning

confidence: 99%

Comparison of Physicochemical Studies of Single Tailed and Gemini Cyclohexanoxy Carbonyl Pyridinium Cationic Amphiphiles

Aggarwal¹

2017

J Proteomics Bioinform

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In the present research work, the physicochemical studies of surface active Cyclohexanoxy carbonyl Pyridinium single tailed and Gemini amphiphiles had been compared. Thermal stability, size of aggregates in aqueous system and interaction with a globular protein, Bovine Serum Albumin (BSA), was done by using TGA analysis, DLS, UV-visible, steady-state fluorescence and synchronous fluorescence and TEM respectively. On the basis of the experiments, it had been concluded that the Gemini amphiphile possessed less cytotoxicity, high thermally stability, form small sized compact aggregates and stable complex with BSA. The results have further been supported by higher value of Stern-Volmer quenching constant (K SV ) and a higher binding constants for Gemini amphiphiles as compared to single tailed amphiphiles. Moreover, on the basis of synchronous fluorescence spectra and UV spectra, it has been concluded that both the amphiphiles mainly interact with tryptophan residues. The less cytotoxicity values and stabilization of secondary structure of BSA in low concentration of ionic liquids implies that these ionic liquids can replaced the conventional surfactants in the detergent industries and used as a potential vehicles for the drug and gene delivery.the change in the wavelength of emission maximum (λ max ) and intensity parameters found to be sensitive to protein conformation and can be used to investigate the interactions between BSA and ionic liquids. DLS and TEM studies are used to see the change in conformation of the amphiphiles in the presence of BSA. Materials and Methods MaterialsGemini Amphiphiles (GA) and Single Tailed amphiphiles (ST) ( Figure 1) were synthesized in our lab by an earlier reported procedure [18,19]. Bovine Serum Albumin (BSA) (MW=66 kDa) was purchased from Central drug house (New Delhi, India) and was used as received. 0.01 M buffer, pH 7.2, was made from 0.01 M KH 2 PO 4 and 0.01 M sodium hydroxide. Potassium dihydrogen phosphate and sodium hydroxide were purchased from Merck, India. Millipore water was used in all experiments. Thermal gravimetric analysisThermal stability of both the amphiphiles had been investigated by Perkin Elmer Pyris 1 Thermal Gravimetric Analyzer (TGA). Both the samples were completely dried by rotatory vaccum pump. Both the samples were added in to the aluminum pans under the inert atmosphere at a heating rate of 10°C/min. Dynamic Light Scattering (DLS)The size of the studied cationic amphiphiles has been measured by the Zetasizer Nano ZS (Malvern Instrument Ltd.) UK. The inbuilt peltier device controls the temperature with an accuracy of ±0.1 K. The 1.0 mM aqueous solution of both amphiphiles has been filtered through 0.45 μM pore sized filter before measurement. CytotoxicityThe cytotoxicity of, 1.0 mM aqueous solution, both synthesized amphiphiles was carried out on C 6 glioma (cancerous brain cell line, passage number 65) by using MTT assay to calculate the IC 50 value of both the synthesized ionic liquids. Cells were seeded at a density of 10 × 10 3 cells/m...

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“…Where F0 and F are the fluorescence intensities before and after the addition of the quencher, respectively, kq is the bimolecular quenching constant, τ 0 is the average lifetime of the biomolecule (10 -8 s), and [Q] is the concentration of the quencher (22,23). The fluorescence spectroscopy device was a Carry -100 Bio; Varian, Australia, and quartz cells with 10 mm diameter were used.…”

Section: Fluorescence Measurementsmentioning

confidence: 99%

Human Serum Albumin Structure in Presence of Different Concentrations of Cortisol and Glucose: An In Vitro Modeling Under Normal and Hyperglycemic Conditions

Amini-Geram

Goshadrou

Ebrahim‐Habibi

et al. 2016

Iran Red Crescent Med J

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Background: Glucose is an essential element in the supply of body's energy. In diseases such as diabetes, glucose increase is associated with disturbance in metabolism. Cortisol is an important hormone in the regulation of glucose metabolism, and human serum albumin (HSA) is one of the most important glucose and cortisol transmitters in blood. Interaction between albumin and these ligands could affect HSA secondary structure and its stability. Objectives: The aim of this study was to investigate HSA secondary structure in the presence of different concentrations of glucose and cortisol. Methods: This was an in vitro (analytical/descriptive) study in which, completely randomized design was used to study the interaction between human serum albumin

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Spectroscopic Studies on the Interaction of Acid Yellow With Bovine Serum Albumin

Cited by 102 publications

References 38 publications

Study on the interaction of food colourant quinoline yellow with bovine serum albumin by spectroscopic techniques

Study on the interaction of food colourant quinoline yellow with bovine serum albumin by spectroscopic techniques

Comparison of Physicochemical Studies of Single Tailed and Gemini Cyclohexanoxy Carbonyl Pyridinium Cationic Amphiphiles

Human Serum Albumin Structure in Presence of Different Concentrations of Cortisol and Glucose: An In Vitro Modeling Under Normal and Hyperglycemic Conditions

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