Binding of ethyl pyruvate to bovine serum albumin: Calorimetric, spectroscopic and molecular docking studies

Pathak, Mallika; Mishra, Rashmi; Agarwala, Paban K.; Ojha, Himanshu; Singh, Bhawna; Singh, Anju

doi:10.1016/j.tca.2016.04.006

Cited by 47 publications

(18 citation statements)

References 35 publications

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“…Static quenching is controlled by the formation of a complex, thus, as the temperature increases, the static quenching constant decreases due to the lower stability of the complex, whereas the opposite effect is found with dynamic quenching . The maximum rate of dynamic quenching was ~2 × 10 10 L mol − 1 s −1 , and the quenching rate constants were 10 12 L mol −1 s −1 in our experiments, i.e. much higher than the dynamic quenching rate.…”

Section: Resultsmentioning

confidence: 48%

“…Therefore, it was identified as an isobestic point, and only one complex was generated during the combination between C3G and HSA, gHSA. An equilibrium existed between the bound and free forms of protein . These phenomena indicated that the characteristics and conformation of HSA and gHSA were changed on addition of C3G, and we conclude that the structural stability of HSA was altered more easily than that of gHSA.…”

Section: Resultsmentioning

confidence: 69%

“…The data show that the number of binding sites was close to 1, indicating that there was a single binding site on HSA, gHSA for C3G. The K a value reached an order of magnitude of 10 −4 , showing that C3G was able to combine with the proteins . Moreover, the value decreased as the temperature increased.…”

Section: Resultsmentioning

confidence: 88%

“…The results show that there were two peaks in the spectra of HSA and gHSA. The first peak at 206 nm represents absorption of the protein characteristic polypeptide backbone structure –C = O, and the amino acid residue (Phe, Trp, Tyr) characteristic peak was at 280 nm . The wave patterns of pure HSA and gHSA were similar, and the positions and absorbance of the absorption peaks (around 1.86, 0.12 abs) were unchanged in the absence of C3G.…”

Section: Resultsmentioning

confidence: 97%

See 3 more Smart Citations

Spectroscopic andin silicostudy of binding mechanism of cynidine‐3‐O‐glucoside with human serum albumin and glycated human serum albumin

Gao

Jia

et al. 2016

Luminescence

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The drug-serum albumin interaction plays a dominant role in drug efficacy and disposition. The glycation of serum albumin that occurs during diabetes may affect its drug-binding properties in vivo. In order to evaluate the interactivity characteristics of cyanidin-3-O-glucoside (C3G) with human serum albumin (HSA) and glycated human serum albumin (gHSA), this study was undertaken using multiple spectroscopic techniques and molecular modeling analysis. Time-resolved fluorescence and the thermodynamic parameters indicated that the quenching mechanism was static quenching, and hydrogen bonding and Van der Waals force were the main forces. The protein fluorescence could be quenched by C3G, whereas the polarity of the fluorophore was not obviously changed. C3G significantly altered the secondary structure of the proteins. Furthermore, the interaction force that existed in the HSA-C3G system was greater than that in the gHSA-C3G system. Fluorescence excitation emission matrix spectra, red edge excitation shift, Fourier transform infrared spectroscopy and circular dichroism spectra provided further evidence that glycation could inhibit the binding between C3G and proteins. In addition, molecular modeling analysis supported the experimental results. The results provided more details for the application of C3G in the treatment of diabetes.

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Section: Resultsmentioning

confidence: 48%

Section: Resultsmentioning

confidence: 69%

Section: Resultsmentioning

confidence: 88%

Section: Resultsmentioning

confidence: 97%

See 2 more Smart Citations

Spectroscopic andin silicostudy of binding mechanism of cynidine‐3‐O‐glucoside with human serum albumin and glycated human serum albumin

Gao

Jia

et al. 2016

Luminescence

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“…Therefore, it can be inferred that the binding interaction between naphthylchalcone derivative 2a and BSA resulted in enhancement of the hydrophilicity around the Trp residues of BSA. The blue shift suggested that the Trp residue is buried in the hydrophobic environment of the BSA protein, which signifies that binding of the ligands creates a more apolar environment around the Trp residue . Some previous studies have reported the binding of chalcones with serum proteins, but most have reported a blue shift in the wavelength maxima in the fluorescence emission spectra of the serum protein .…”

Section: Resultsmentioning

confidence: 95%

Luminescence, circular dichroism and in silico studies of binding interaction of synthesized naphthylchalcone derivatives with bovine serum albumin

et al. 2017

Self Cite

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Chalcones possess various biological properties, for example, antimicrobial, anti-inflammatory, analgesic, antimalarial, anticancer, antiprotozoal and antitubercular activity. In this study, naphthylchalcone derivatives were synthesized and characterized using H NMR C NMR, Fourier transform infrared and mass techniques. Yields for all derivatives were found to be >90%. Protein-drug interactions influence the absorption, distribution, metabolism and excretion (ADME) properties of a drug. Therefore, to establish whether the synthesized naphthylchalcone derivatives can be used as drugs, their binding interaction toward a serum protein (bovine serum albumin) was investigated using fluorescence, circular dichroism and molecular docking techniques under physiological conditions. Fluorescence quenching of the protein in the presence of naphthylchalcone derivatives, and other derived parameters such as association constants, number of binding sites and static quenching involving confirmed non-covalent binding interactions in the protein-ligand complex were observed. Circular dichroism clearly showed changes in the secondary structure of the protein in the presence of naphthylchalcones, indicating binding between the derivatives and the serum protein. Molecular modelling further confirmed the binding mode of naphthylchalcone derivatives in bovine serum albumin. A site-specific molecular docking study of naphthylchalcone derivatives with serum albumin showed that binding took place primarily in the aromatic low helix and then in subdomain II. The dominance of hydrophobic, hydrophilic and hydrogen bonding was clearly visible and was responsible for stabilization of the complex.

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Insights into the interaction of methotrexate and human serum albumin: A spectroscopic and molecular modeling approach

et al. 2017

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In this study, fluorescence spectroscopy and molecular modeling approaches were employed to investigate the binding of methotrexate to human serum albumin (HSA) under physiological conditions. From the mechanism, it was demonstrated that fluorescence quenching of HSA by methotrexate results from the formation of a methotrexate/HSA complex. Binding parameters calculated using the Stern-Volmer method and the Scatchard method showed that methotrexate binds to HSA with binding affinities in the order 10 L·mol . Thermodynamic parameter studies revealed that the binding reaction is spontaneous, and that hydrogen bonds and van der Waals interactions play a major role in the reaction. Site marker competitive displacement experiments and a molecular modeling approach demonstrated that methotrexate binds with appropriate affinity to site I (subdomain IIA) of HSA. Furthermore, we discuss some factors that influence methotrexate binding to HSA.

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Binding of ethyl pyruvate to bovine serum albumin: Calorimetric, spectroscopic and molecular docking studies

Cited by 47 publications

References 35 publications

Spectroscopic andin silicostudy of binding mechanism of cynidine‐3‐O‐glucoside with human serum albumin and glycated human serum albumin

Spectroscopic andin silicostudy of binding mechanism of cynidine‐3‐O‐glucoside with human serum albumin and glycated human serum albumin

Luminescence, circular dichroism and in silico studies of binding interaction of synthesized naphthylchalcone derivatives with bovine serum albumin

Insights into the interaction of methotrexate and human serum albumin: A spectroscopic and molecular modeling approach

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