Munmun Bardhan

A detailed spectroscopic study on the interaction of Rhodamine 6G with human hemoglobin.

UV-vis, time-resolved fluorescence and circular dichroism spectroscopic investigations have been made to reveal the nature of the interactions between xanthene dye Rhodamine 6G and the well known protein hemoglobin. From the analysis of the steady-state and time-resolved fluorescence quenching of Rhodamine 6G in aqueous solutions in presence of hemoglobin, it is revealed that the quenching is static in nature. The primary binding pattern between Rhodamine and hemoglobin has been interpreted as combined effect of hydrophobic association and electrostatic interaction. The binding constants, number of binding sites and thermodynamic parameters at various pH of the environment have been computed. The binding average distance between the energy donor Rhodamine and acceptor hemoglobin has been determined from the Forsters theory.

Interaction of bovine serum albumin and albumin-gold nanoconjugates with l-aspartic acid. A spectroscopic approach

The interaction of an essential transport protein bovine serum albumin (BSA) and albumin-gold nanoconjugates (BSA-GNPs) with amino acid l-aspartic (ASP) are investigated by steady state and time resolved spectroscopic techniques. In both the cases, static fluorescence quenching is observed indicating that a ground state complex is formed between the donor BSA/BSA-GNP with the acceptor ASP. High values of quenching constant suggest that energy transfer also occurred from BSA and BSA-GNPs to ASP. Distance between the fluorophore in the protein and the amino acid (ASP) is evaluated. Binding constants and the number of binding sites were determined in both the cases. The observed thermodynamic parameters suggest that the key interacting forces involved in both cases are hydrophobic interactions. Circular dichroism (CD) spectrum of BSA molecule suffers marginal change in the presence of ASP both in its pure as well as bio-nanoconjugate forms. As no structural deformation is occurred, the biological activity along with the activity of immune response of protein and the biocompatibility of protein-nanoconjugate remain as such.

Investigations on the interactions of aurintricarboxylic acid with bovine serum albumin: Steady state/time resolved spectroscopic and docking studies

In this paper, the nature of the interactions between bovine serum albumin (BSA) and aurintricarboxylic acid (ATA) has been investigated by measuring steady state and time-resolved fluorescence, circular dichroism (CD), FT-IR and fluorescence anisotropy in protein environment under physiological conditions. From the analysis of the steady state and time-resolved fluorescence quenching of BSA in aqueous solution in presence of ATA it has been inferred that the nature of the quenching originates from the combined effect of static and dynamic modes. From the determination of the thermodynamic parameters obtained from temperature-dependent changes in K(b) (binding constant) it was apparent that the combined effect of hydrophobic association and electrostatic attraction is responsible for the interaction of ATA with BSA. The effect of ATA on the conformation of BSA has been examined by analyzing CD spectrum. Though the observed results demonstrate some conformational changes in BSA in presence of ATA but the secondary structure of BSA, predominantly of α-helix, is found to retain its identity. Molecular docking of ATA with BSA also indicates that ATA docks through hydrophobic interaction.

Steady state, time resolved, and circular dichroism spectroscopic studies to reveal the nature of interactions of zinc oxide nanoparticles with transport protein bovine serum albumin and to monitor the possible protein conformational changes

In this paper, the interaction between bovine serum albumin (BSA) and zinc oxide (ZnO) nanoparticles was investigated by fluorescence quenching spectra, circular dichroism (CD), and synchronous spectra under physiological conditions. From the analysis of the steady state and time resolved fluorescence quenching of BSA in aqueous solution in presence of ZnO it was observed that the nature of the quenching is of static-type quenching. The Stern–Volmer quenching constant KS at different temperatures were determined and the thermodynamic parameters ΔH, ΔG, and ΔS were computed. The experiment revealed that the electrostatic interaction was the predominant force in stabilizing the complex. The effect of ZnO on the conformation of BSA has been analyzed by synchronous spectra and CD spectrum. Although the observed results demonstrate some conformational changes in BSA in presence of ZnO nanoparticles, the secondary structure of BSA, predominantly of α-helix, is found to retain its identity.

To reveal the nature of interactions of human hemoglobin with gold nanoparticles having two different morphologies (sphere and star-shaped) by using various spectroscopic techniques

The nature of interactions between heme protein human hemoglobin (HHb) and gold nanoparticles of two different morphologies that is GNP (spherical) and GNS (star-shaped) have been investigated by using UV-vis absorption, steady state fluorescence, synchronous fluorescence, resonance light scattering (RLS), time resolved fluorescence, FT-IR, and circular dichroism (CD) techniques under physiological condition of pH ~7 at ambient and different temperatures. Analysis of the steady state fluorescence quenching of HHb in aqueous solution in the presence of GNP and GNS suggests that the nature of the quenching is of static type. The static nature of the quenching is also confirmed from time resolved data. The static type of quenching also indicates the possibility of formation of ground state complex for both HHb-GNP and HHb-GNS systems. From the measurements of Stern-Volmer (SV) constants KSV and binding constants, KA and number of binding sites it appears that HHb forms stronger binding with GNP relative to GNS. Analysis of the thermodynamic parameters indicates that the formation of HHb-GNP and HHb-GNS complexes are spontaneous molecular interaction processes (∆G<0). In both cases hydrogen bonding and van der Waals interactions play a dominant role (∆H<0, ∆S<0). Synchronous fluorescence spectroscopy further reveals that the ground state complex formations of HHb-GNP and HHb-GNS preferably occur by binding with the amino acid tyrosine through hydrogen bonding interactions. Moreover the α-helicity contents of the proteins as obtained from the circular dichroism (CD) spectra appears to be marginally reduced by increasing concentrations of GNP and GNS and the α-helical structures of HHb retain its identity as native secondary structure in spite of complex formations with GNP or GNS. These findings demonstrate the efficiency of biomedical applications of GNP and GNS nanoparticles as well as in elucidating their mechanisms of action as drugs or drug delivery systems in human.

Investigations on the Photoreactions of Phenothiazine and Phenoxazine in Presence of 9-cyanoanthracene by Using Steady State and Time Resolved Spectroscopic Techniques

By using electrochemical, steady state and time resolved (fluorescence lifetime and transient absorption) spectroscopic techniques, detailed investigations were made to reveal the mechanisms of charge separation or forward electron transfer reactions within the electron donor phenothiazine (PTZH) or phenoxazine (PXZH) and well known electron acceptor 9-cyanoanthracene (CNA). The transient absorption spectra suggest that the charge separated species formed in the excited singlet state resulted from intermolecular photoinduced electron transfer reactions within the donor PTZH (or PXZH) and CNA acceptor relaxes to the corresponding triplet state. Though alternative mechanisms of via formations of contact neutral radical by H-transfer reaction have been proposed but the observed results obtained from the time resolved measurements indicate that the regeneration of ground state reactants is primarily responsible due to direct recombination of triplet contact ion-pair (CIP) or solvent-separated ion-pair (SSIP).