Vishwas D. Suryawanshi

Publications (3)7.29 Total impact

• Article: Spectroscopic Investigation on the Interaction of Pyrimidine Derivative, 2-Amino-6-hydroxy-4-(3,4-dimethoxyphenyl)-pyrimidine-5-carbonitrile with Human Serum Albumin: Mechanistic and Conformational Study

  Vishwas D. Suryawanshi, Prashant V. Anbhule, Anil H. Gore, Shivajirao R. Patil, Govind B. Kolekar
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  ABSTRACT: In the present study, fluorescence spectroscopy in combination with UV–vis absorption spectroscopy and synchronous fluorescence spectroscopy (SFS) was employed to investigate the binding affinity of pyrimidine derivative, 2-amino-6-hydroxy-4-(3,4-dimethoxyphenyl)-pyrimidine-5-carbonitrile (AHDMPPC) to human serum albumin (HSA) under the physiological conditions. In the mechanism discussion, it was proved that the fluorescence quenching of HSA by AHDMPPC is a result of the formation of AHDMPPC–HSA complex. The quenching mechanism and number of binding sites (n ≈ 1) were obtained by fluorescence titration data. Binding parameters calculated from Stern–Volmer method showed that the AHDMPPC bind to HSA with the binding affinities of the order 104 L mol–1. The thermodynamic parameters studies revealed that the binding was characterized by negative enthalpy and positive entropy changes −13.06 kJ/mol and 51.34 J/mol K–1 (from the Van’t Hoff equation) and suggest that the binding reaction was exothermic and hydrophobic interaction is the predominant intermolecular forces stabilizing the complex. The specific binding distance (r = 2.25 nm) between donor HSA and acceptor AHDMPPC was obtained according to fluorescence resonance energy transfer (FRET). Furthermore, the synchronous spectral result, three–dimensional fluorescence spectra and circular dichroism (CD) indicates that the secondary structure of HSA was changed in the presence of AHDMPPC.
  Industrial & Engineering Chemistry Research 12/2012; 51(1):95–102. · 2.24 Impact Factor
• Article: Micellar-mediated binding interaction between perylene and dl-phenylalanine: Insights from spectroscopic investigations

  Vishwas D. Suryawanshi, Prashant V. Anbhule, Anil H. Gore, Shivajirao R. Patil, Govind B. Kolekar
  [show abstract] [hide abstract]
  ABSTRACT: In the present study, fluorescence spectroscopy in combination with UV–vis absorption spectroscopy and synchronous fluorescence spectroscopy (SFS) was employed to investigate the binding affinity of pyrimidine derivative, 2-amino-6-hydroxy-4-(3,4-dimethoxyphenyl)-pyrimidine-5-carbonitrile (AHDMPPC) to human serum albumin (HSA) under the physiological conditions. In the mechanism discussion, it was proved that the fluorescence quenching of HSA by AHDMPPC is a result of the formation of AHDMPPC–HSA complex. The quenching mechanism and number of binding sites (n ≈ 1) were obtained by fluorescence titration data. Binding parameters calculated from Stern–Volmer method showed that the AHDMPPC bind to HSA with the binding affinities of the order 104 L mol–1. The thermodynamic parameters studies revealed that the binding was characterized by negative enthalpy and positive entropy changes −13.06 kJ/mol and 51.34 J/mol K–1 (from the Van’t Hoff equation) and suggest that the binding reaction was exothermic and hydrophobic interaction is the predominant intermolecular forces stabilizing the complex. The specific binding distance (r = 2.25 nm) between donor HSA and acceptor AHDMPPC was obtained according to fluorescence resonance energy transfer (FRET). Furthermore, the synchronous spectral result, three–dimensional fluorescence spectra and circular dichroism (CD) indicates that the secondary structure of HSA was changed in the presence of AHDMPPC.
  Industrial & Engineering Chemistry Research 12/2012; 51(1-DOI: 10.1021/ie202005c):95–102. · 2.24 Impact Factor
• Article: A spectral deciphering the perturbation of model transporter protein (HSA) by antibacterial pyrimidine derivative: Pharmacokinetic and biophysical insights

  Vishwas D. Suryawanshi, Prashant V. Anbhule, Anil H. Gore, Shivajirao R. Patil, Govind B. Kolekar
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  ABSTRACT: Steady state fluorescence and UV–vis absorption spectroscopic techniques have been exploited to explore the binding interaction of a antibacterial pyrimidine derivative 2-amino-6-hydroxy-4-(4-hydroxyphenyl)- pyrimidine-5-carbonitrile (AHHPPC) with the model transporter protein, human serum albumin (HSA) under the physiological conditions. It exhibits antibacterial activity against Escherichia coli and Staphylococcus aureus. Analysis of fluorescence quenching data of HSA at different temperatures using Stern–Volmer methods revealed the formation of AHHPPC–HSA complex with binding affinities of the order 104 M�1. The binding site number (n � 1) and corresponding thermodynamic parameters (DG), (DH) and (DS) were calculated, indicated that binding reaction was endothermic and the hydrophobic interactions plays a major role in stabilizing the complex. The binding distance (r = 3.13 nm) between donor (HSA) and acceptor (AHHPPC) was obtained according to FRET. Changes in the albumin secondary structure imparted by the compound was confirmed using synchronous fluorescence, electronic absorption, circular dichroism (CD) and three-dimensional (3D) fluorescence spectroscopy. All these experimental results clarified that AHHPPC could bind to HSA and be effectively transported and eliminated in body, which could be a useful guideline for further drug design.
  Journal of Photochemistry and Photobiology B Biology 10/2012; 118:1-8. · 2.81 Impact Factor