Sudip Chakraborty

Pt nanoparticle-based highly sensitive platform for the enzyme-free amperometric sensing of H2O2

Highly sensitive electrochemical platform based on polymer supported Pt nanoparticles (nPts) for the amperometric sensing of H(2)O(2) at sub-nanomolar level without any redox mediator or enzyme is developed. The nPts are generated by the chemical reduction of precursor pre-organized on the electrode surface and characterized by field emission scanning electron microscopy, X-ray diffraction, spectral and electrochemical measurements. The cationic polymer poly(diallyldimethylammonium) chloride was used to assist the pre-organization of metal precursor. nPts on the electrode surface have an average size of 17 nm. The nanoparticles show excellent electrocatalytic activity towards oxidation of H(2)O(2) at less positive potential than the polycrystalline Pt electrode. Unlike the polycrystalline Pt electrode, the nanoparticle-based electrode does not undergo deactivation by surface oxides and other species in solution. Particle loading on the electrode surface controls the electrocatalytic activity. The nanoparticle-based electrode is highly sensitive (9.15 microA/mM) and display linear response up to 3 mM. It could detect 0.5 nM (S/N=5) of H(2)O(2) under hydrodynamic condition in neutral solution and the electrode is highly stable. The detection limit achieved is significantly lower than the other nanoparticle-based electrodes. The excellent performance of the electrode is ascribed to the good catalytic activity of the particle and ensemble behavior of the nanoparticle-modified electrode. The analytical performance of the electrode in the development of glucose biosensor is demonstrated. The biosensor is used for the sensing of glucose in the micromolar level in neutral pH.

Coupling between hydration layer dynamics and unfolding kinetics of HP-36.

We have performed atomistic molecular dynamics simulations of aqueous solutions of HP-36 at 300 K in its native state, as well as at high temperatures to explore the unfolding dynamics of the protein and its correlation with the motion of water around it. On increasing the temperature a partially unfolded molten globule state is formed where the smallest alpha helix (helix 2) unfolds into a coil. It is observed that the unfolding is initiated around the residue Phe-18 which shows a sharp displacement during unfolding. We have noticed that the unfolding of the protein affects the density of water near the protein surface. Besides, the dynamics of water in the protein hydration layer has been found to be strongly correlated with the time evolution of the unfolding process. We have introduced and calculated a displacement time correlation function to monitor the change in water motion relative to the protein backbone during unfolding. We find that the unfolding of helix 2 is associated with an increase in mobility of water around it as compared to water around the other two helices. We have also explored the microscopic aspects of secondary structure specific and site specific solvation dynamics of the protein. The calculations reveal that unfolding influences the solvation dynamics of the protein molecule in a heterogeneous manner depending on the location of the polar probe residues. This seems to be in agreement with recent experimental findings.

Dynamics of Water in the Hydration Layer of a Partially Unfolded Structure of the Protein HP-36

Atomistic molecular dynamics simulations of the folded native structure and a partially unfolded molten globule structure of the protein villin headpiece subdomain or HP-36 have been carried out with explicit solvent to explore the effects of unfolding on the dynamical behavior of water present in the hydration layers of different segments (three alpha-helices) of the protein. The calculations revealed that the unfolding of helix-2 influences the translational and rotational motions of water present in the hydration layers of the three helices in a heterogeneous manner. It is observed that a correlation exists between the unfolding of helix-2 and the microscopic kinetics of protein-water hydrogen bonds formed by its residues. This in turn has an influence on the rigidity of the hydration layers of the helices in the unfolded structure versus that in the folded native structure. These results should provide a microscopic explanation to recent solvation dynamics experiments on folded native and unfolded structures of proteins.

Confined Water: Structure, Dynamics, and Thermodynamics

Understanding the properties of strongly confined water is important for a variety of applications such as fast flow and desalination devices, voltage generation, flow sensing, and nanofluidics. Confined water also plays an important role in many biological processes such as flow through ion channels. Water in the bulk exhibits many unusual properties that arise primarily from the presence of a network of hydrogen bonds. Strong confinement in structures such as carbon nanotubes (CNTs) substantially modifies the structural, thermodynamic, and dynamic (both translational and orientational) properties of water by changing the structure of the hydrogen bond network. In this Account, we provide an overview of the behavior of water molecules confined inside CNTs and slit pores between graphene and graphene oxide (GO) sheets. Water molecules confined in narrow CNTs are arranged in a single file and exhibit solidlike ordering at room temperature due to strong hydrogen bonding between nearest-neighbor molecules. Although molecules constrained to move along a line are expected to exhibit single-file diffusion in contrast to normal Fickian diffusion, we show, from a combination of molecular dynamics simulations and analytic calculations, that water molecules confined in short and narrow CNTs with open ends exhibit Fickian diffusion because of their collective motion as a single unit due to strong hydrogen bonding. Confinement leads to strong anisotropy in the orientational relaxation of water molecules. The time scale of relaxation of the dipolar correlations of water molecules arranged in a single file becomes ultraslow, of the order of several nanoseconds, compared with the value of 2.5 ps for bulk water. In contrast, the relaxation of the vector that joins the two hydrogens in a water molecule is much faster, with a time scale of about 150 fs, which is about 10 times shorter than the corresponding time scale for bulk water. This is a rare example of confinement leading to a speedup of orientational dynamics. The orientational relaxation of confined water molecules proceeds by angular jumps between two locally stable states, making the relaxation qualitatively different from that expected in the diffusive limit. The spontaneous entry of water inside the hydrophobic cavity of CNTs is primarily driven by an increase in the rotational entropy of water molecules inside the cavity, arising from a reduction in the average number of hydrogen bonds attached to a water molecule. From simulations using a variety of water models, we demonstrate that the relatively simple SPC/E water model yields results in close agreement with those obtained from polarizable water models. Finally, we provide an account of the structure and thermodynamics of water confined in the slit pore between two GO sheets with both oxidized and reduced parts. We show that the potential of mean force for the oxidized part of GO sheets in the presence of water exhibits two local minima, one corresponding to a dry cavity and the other corresponding to a fully hydrated cavity. The coexistence of these two regimes provides permeation pathways for water in GO membranes.

Secondary Structure Specific Entropy Change of a Partially Unfolded Protein Molecule

The conformational disorder of a protein in its partially unfolded molten globule (MG) form leads to an overall gain in the configurational entropy of the protein molecule. However, considering the differential degree of unfolding of different secondary structural segments of the protein, the entropy gained by them may be nonuniform. In this work, our attempt has been to explore whether any correlation exists between the degree of unfolding of different segments of a protein and their entropy gains. For that, we have carried out atomistic molecular dynamics simulations of the folded native and a partially unfolded structures of the protein villin headpiece subdomain or HP-36 in aqueous medium. It is found that among the three alpha-helical segments of the protein, the central alpha-helix (helix-2) underwent unfolding during the transition with a consequent entropy gain significantly higher than that of the other two helical segments. The calculations further revealed that the differential entropy gain by the segments of a protein can be used as an effective measure to identify the unfolded segments of the protein and hence to explore the folding pathways.