Interaction of Lysozyme with Rhodamine B: A combined analysis of spectroscopic &amp; molecular docking

Millan, Sabera; Satish, Lakkoji; Kesh, Sandeep; Chaudhary, Yatendra S.; Sahoo, Harekrushna

doi:10.1016/j.jphotobiol.2016.06.047

Cited by 67 publications

(28 citation statements)

References 59 publications

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“…Although the fluorescence quenching was dynamic in nature, static quenching through the ground state complex formation cannot be ignored as the complex formation between BSA and ILs observed from absorbance studies. When small molecules bind independently to a set of equivalent sites of a biomolecule, the equilibrium between free and bound molecules is given by the following, equation (2)

italiclog \frac{F_{0} - F}{F} = italiclog K_{b} + n italiclog ([],, Q)

where, n is the number of binding sites and K b is the binding constant. The values of n and K b were obtained from the slope and intercept of the plot of log(F 0 ‐ F)/F 0 versus log[Q] respectively (Figure S1) The results for the three ILs at different temperatures (298, 301, 304 and 307 K) are given in Table .…”

Section: Resultsmentioning

confidence: 99%

Spectroscopic insight into the interaction of bovine serum albumin with imidazolium‐based ionic liquids in aqueous solution

2016

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The study of protein–ionic liquid interactions is very important because of the widespread use of ionic liquids as protein stabilizer in the recent years. In this work, the interaction of bovine serum albumin (BSA) with different imidazolium‐based ionic liquids (ILs) such as [1‐ethyl‐3‐methyl‐imidazolium ethyl sulfate (EmimESO4), 1‐ethyl‐3‐methyl‐imidazolium chloride (EmimCl) and 1‐butyl‐3‐methyl‐imidazolium chloride (BmimCl)] has been investigated using different spectroscopic techniques. The intrinsic fluorescence of BSA is quenched by ILs by the dynamic mechanism. The thermodynamic analysis demonstrates that very weak interactions exist between BSA and ILs. 8‐Anilino‐1‐naphthalenesulfonic acid (ANS) fluorescence and lifetime measurements reveal the formation of the compact structure of BSA in IL medium. The conformational changes of BSA were monitored by CD analysis. Temperature‐dependent ultraviolet (UV) measurements were done to study the thermal stability of BSA. The thermal stability of BSA in the presence of ILs follows the trend EmimESO4 > EmimCl > BmimCl and in the presence of more hydrophobic IL, destabilization increases rapidly as a function of concentration.

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italiclog \frac{F_{0} - F}{F} = italiclog K_{b} + n italiclog ([],, Q)

Section: Resultsmentioning

confidence: 99%

Spectroscopic insight into the interaction of bovine serum albumin with imidazolium‐based ionic liquids in aqueous solution

2016

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“…decrease in fluorescence intensity) is very convenient to explore the nature and binding mechanism of the protein–ligand complex. The ligand molecules quenched the protein fluorescence by a range of molecular interaction processes such as molecular rearrangement, excited‐state reactions, energy transfer, ground‐state complex formation or collisional quenching BSA emission spectra in the absence or presence of various concentrations of CuFe 2 O 4 NP (displayed in Figure ) indicated that the fluorescence intensity of BSA gradually decreased with the addition of different concentrations of CuFe 2 O 4 NP, but there was no significant wavelength shift observed in the emission maximum. This result suggested that the interaction between BSA and CuFe 2 O 4 NP occurred and the polarity in the microenvironment near the Trp residue was not affected by this interaction …”

Section: Resultsmentioning

confidence: 99%

“…Far‐UV (190–250 nm) CD measurement provides information about the possible changes in the secondary structure of protein upon interaction with small ligand molecules . The two negative bands at 208 and 222 nm referred to the characteristic peaks for the BSA α‐helical structure .…”

Section: Resultsmentioning

confidence: 99%

Insights into the binding interaction between copper ferrite nanoparticles and bovine serum albumin: An effect on protein conformation and activity

et al. 2018

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The binding affinity between bovine serum albumin (BSA) and copper ferrite (CuFe O ) nanoparticles in terms of conformation, stability and activity of protein was studied using various spectroscopic methods. The quenching involved in BSA-CuFe O NP interaction was static quenching as analysed by different techniques (steady-state and time-resolved fluorescence along with temperature-dependent fluorescence measurements). Among all types of possible interactions, it was revealed that the major binding forces were van der Waals interaction and hydrogen bonding, which were explored from negative values of enthalpy change (∆H = -193.85 kJ mol ) and entropy change (∆S = -588.88 J mol K ). Additionally, synchronous, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy measurements confirmed the conformational changes in BSA upon the addition of CuFe O NP. Furthermore, thermal denaturation observations were consistent with the circular dichroism results. The interaction of CuFe O NP with BSA decreased the esterase activity in the BSA assay, revealing the affinity of copper ferrite towards the active site of BSA.

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“…The CD shows no apparent change between pH 7.59 and 11.10 (Figure3B), indicating that Lys retains all the features of secondary structure found in the native protein. However, at pH 12.13, two peaks decrease obviously to a minimum value ( Figure 3B), which suggest that the secondary structure of Lys was unfolded partially [25,26]. Thus, from pH 2.55 to 11.10, the tertiary structure of Lys altered but its secondary structure did not unfold obviously until pH up to 12.13, which may be the reason for the potential change in Figure 2A.…”

Section: Protein Conformationmentioning

confidence: 94%

“…Lys contains six tryptophan (Trp) residues and three tyrosine (Tyr) residues (inset in Figure3A). Among Trp residues, Trp 28 108, 111, and 123 residues are present in the -domain, and Trp 62 and 63 residues are located at the hinge region between  and domains of the protein [25]. Trp 62 and 108 residues are partially exposed to the solvent and not close to cystine or methionine sulfurs, which are responsible for the most intrinsic fluorescence of native Lys and reflect the conformational alteration of protein [20].…”

Section: Protein Conformationmentioning

confidence: 99%

pH-Controllable Bioelectrocatalysis Based on Surface Charge and Conformation Switching of Nonelectroactive Protein

Wu¹

2018

International Journal of Electrochemical Science

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Lysozyme (Lys), a nonelectroactive protein, was covalently bonded with L-cysteine (L-Cys) selfassembled monolayers (SAMs) on Au electrode to obtain the pH-switchable interface (Lys/L-Cys). Based on the surface charge and conformational switching of Lys at pH 6.19 and 12.13, the Lys/LCys/Au electrode exhibited a pH-sensitive onoff behavior toward the electroactive probe of Fe(CN) 6 3 . As pH was lower or higher than the isoelectronic point (pI 11.0) of Lys, Lys on electrode was positively or negatively charged by the protonation or deprotonation of amino acid residues. Furthermore, protein conformation was reversibly folded or unfolded to the native state and unfolded intermediate accordingly. Consequently, the electrostatic force between Lys and probe of Fe(CN) 6 3 and reversible conformational change of Lys are responsible for the pH-sensitive onoff behavior of Lys/L-Cys/Au interface. Moreover, the switchable properties of Lys/L-Cys/Au electrode were used to realize pH-controlled electrochemical reduction of H 2 O 2 and exhibited high sensitivity for the bioelectrocatalytic reduction of H 2 O 2 . In the linear range of 0.211.2 mM, the response sensitivity was calculated to be 379 A mM 1 cm 2 . The investigations in the mechanism for pH-sensitive behavior and electrocatalysis of the interface suggest that the nonelectroactive Lys/L-Cys film provides potential for fabricating novel switchable electrochemical biosensors and bioelectronic devices.

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Interaction of Lysozyme with Rhodamine B: A combined analysis of spectroscopic & molecular docking

Cited by 67 publications

References 59 publications

Spectroscopic insight into the interaction of bovine serum albumin with imidazolium‐based ionic liquids in aqueous solution

Spectroscopic insight into the interaction of bovine serum albumin with imidazolium‐based ionic liquids in aqueous solution

Insights into the binding interaction between copper ferrite nanoparticles and bovine serum albumin: An effect on protein conformation and activity

pH-Controllable Bioelectrocatalysis Based on Surface Charge and Conformation Switching of Nonelectroactive Protein

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