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Shivamurti A. Chimatadar

Bio: Shivamurti A. Chimatadar is an academic researcher from Karnatak University. The author has contributed to research in topics: Reaction rate & Aqueous solution. The author has an hindex of 17, co-authored 113 publications receiving 1234 citations.


Papers
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TL;DR: Spectroscopic analysis of the emissionQuenching at different temperatures revealed that the quenching mechanism of serum albumin by dexamethasone is static quench mechanism.
Abstract: This study was designed to examine the interaction of dexamethasone (DEX) with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions with drug concentrations in the range of 2.5-20 microM and BSA/HSA was fixed at 5.0 microM. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of serum albumin by dexamethasone is static quenching mechanism. The binding sites number, n and binding constant, K were obtained at various temperatures. The distance r between dexamethasone and the protein was evaluated according to the theory of Foster energy transfer. The result of fluorescence spectra UV-vis absorption spectra and FT-IR spectra showed that the conformation of bovine serum albumin and human serum albumin has been changed in the presence of dexamethasone. The thermodynamic parameters, free energy change (DeltaG(0)), enthalpy change (DeltaH(0)) and entropy change (DeltaS(0)) for BSA-DEX and HSA-DEX were calculated according to van't Hoff equation and discussed.

202 citations

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TL;DR: The binding of sulfamethoxazole (SMZ) to bovine serum albumin (BSA) was investigated by spectroscopic methods viz., fluorescence, FT-IR and UV-vis absorption techniques and showed the binding of SMZ to BSA induced conformational changes in BSA.

84 citations

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TL;DR: A molecular modeling study further confirmed the binding mode obtained by the experimental studies, and was proposed to be Sudlow’s site I based on displacement experiments using site markers viz. warfarin, ibuprofen and digitoxin.

64 citations

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TL;DR: Molecular docking study confirms the drug binding sites and interaction of hydralazine with amino acid residues and confirms the involvement of hydrogen bonding with weak van der Waals forces in the interaction.
Abstract: Biomolecular interaction of hydralazine with human serum albumin (HSA) was studied by fluorescence, ultravoilet, three-dimensional, synchronous, Fourier transform infrared, lifetime fluorescence, resonance Rayleigh scattering, circular dichroism, and molecular docking techniques. The intrinsic fluorescence of HSA was quenched by a static quenching mechanism. The effect of β-cyclodextrin on binding was studied. Binding constants and number of binding sites were evaluated using the Stern–Volmer equation. Thermodynamic parameters (ΔH°, ΔG°, and ΔS°) indicate the involvement of hydrogen bonding with weak van der Waals forces in the interaction. The average binding distance (r) between the HSA and hydralazine was calculated by Fourier resonance energy transfer theory. Molecular docking study confirms the drug binding sites and interaction of hydralazine with amino acid residues.

61 citations

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TL;DR: The circular dichroism data revealed that the presence of EPN decreased the α–helix content of serum albumin, which indicated conformation changes in HSA upon interaction with EPN, according to the Forster's theory of non–radiation energy transfer.

49 citations


Cited by
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Journal ArticleDOI
TL;DR: The review highlights the main achievements reported in the last 3 years: harnessing the casein micelle, a natural nanovehicle of nutrients, for delivering hydrophobic bioactives, and discovering unique nanotubes based on enzymatic hydrolysis of α-la.
Abstract: Milk proteins are natural vehicles for bioactives. Many of their structural and physicochemical properties facilitate their functionality in delivery systems. These properties include binding of ions and small molecules, excellent surface and self-assembly properties; superb gelation properties; pH-responsive gel swelling behavior, useful for programmable release; interactions with other macromolecules to form complexes and conjugates with synergistic combinations of properties; various shielding capabilities, essential for protecting sensitive payload; biocompatibility and biodegradability, enabling to control the bioaccessibility of the bioactive, and promote its bioavailability. The review highlights the main achievements reported in the last 3 years: harnessing the casein micelle, a natural nanovehicle of nutrients, for delivering hydrophobic bioactives; discovering unique nanotubes based on enzymatic hydrolysis of α-la; introduction of novel encapsulation techniques based on cold-set gelation for delivering heat-sensitive bioactives including probiotics; developments and use of Maillard reaction based conjugates of milk proteins and polysaccharides for encapsulating bioactives; introduction of β-lg–pectin nanocomplexes for delivery of hydrophobic nutraceuticals in clear acid beverages; development of core-shell nanoparticles made of heat-aggregated β-lg, nanocoated by beet-pectin, for bioactive delivery; synergizing the surface properties of whey proteins with stabilization properties of polysaccharides in advanced W/O/W and O/W/O double emulsions; application of milk proteins for drug targeting, including lactoferrin or bovine serum albumin conjugated nanoparticles for effective in vivo drug delivery across the blood-brain barrier; beta casein nanoparticles for targeting gastric cancer; fatty acid-coated bovine serum albumin nanoparticles for intestinal delivery, and Maillard conjugates of casein and resistant starch for colon targeting. Major future challenges are spot-lighted.

857 citations

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TL;DR: The feasibility of using thermally activated persulfate (TAP) to degrade chloramphenicol (CAP) in aqueous solution was evaluated in this paper, and the observed rate constants well fitted the Arrhenius equation.

361 citations

Journal ArticleDOI
TL;DR: It was proposed that kaempferol may interact with some amino acid residues located within the active site of α-glucosidase, occupying the catalytic center of the enzyme to avoid the entrance of p-nitrophenyl-α-D- glucopyranoside and ultimately inhibiting the enzyme activity.

249 citations

01 Jan 2016

241 citations

Journal ArticleDOI
TL;DR: Glycerol is a highly versatile molecule because of its three hydroxyl groups and can be transformed to a plethora of different value-added fine chemicals and products as mentioned in this paper, and it is an important byproduct...
Abstract: Glycerol is a highly versatile molecule because of its three hydroxyl groups and can be transformed to a plethora of different value-added fine chemicals and products. It is an important byproduct ...

206 citations