Journal of Biophysical Chemistry 

About: Journal of Biophysical Chemistry is an academic journal published by Scientific Research Publishing. The journal publishes majorly in the area(s): Docking (molecular) & Circular dichroism. It has an ISSN identifier of 2153-036X. It is also open access. Over the lifetime, 187 publications have been published receiving 1631 citations. The journal is also known as: JBPC.

Cancer chemoprevention through the induction of apoptosis by natural compounds

Abstract: As cell and tissue homeostasis are mediated by the balance between proliferation and apoptosis, controlling this balance is important for cancer chemoprevention. Cancer chemoprevention can be achieved by the use of natural, synthetic or biologic compounds that reverse, suppress or prevent the development of epithelial malignancies. Natural compounds including flavonoids are able to reduce oxidative stress, which is the most likely mechanism mediating the protective effects against cancer development. In addition, in vitro and in vivo studies have suggested that flavonoids, such as (-)-epigallocatechin-3-gallete (EGCG), quercetin, and curcumin, act by induction of apoptosis. Several natural compounds inhibit cell proliferation and angiogenesis. Certain natural products have been shown to inhibit the activation of nuclear factor kappa B (NF-κB) and Akt signaling pathways, both of which are known to maintain a homeostatic balance between cell survival and apoptosis. Understanding the mechanism of these natural products will contribute to the development of more specific preventive strategies against cancer development. Here we focus on the ability of natural cancer chemopreventive agents to induce apoptosis, and attempt to provide evidence for the preventive and therapeutic effects of natural compounds, EGCG, quercetin, and curcumin, in a succinct manner highlightingκand Akt signaling pathways in vivo.

A spectroscopic study of the interaction of the antioxidant naringin with bovine serum albumin

Abstract: The interaction of naringin with bovine serum albumin has been performed using fluorescence, circular dichroism and fourier transform infrared spectroscopy in 20 mM phosphate buffer of pH 7.0 as well as molecular docking studies. The changes in enthalpy (ΔH°) and entropy (ΔS°) of the interaction were found to be +18.73 kJ/mol and +143.64 J mol-1 K-1 respectively, indicating that the interaction of naringin with bovine serum albumin occurred mainly through hydrophobic interactions. Negative values of free energy change (ΔG°) at different temperatures point toward the spontaneity of the interaction. Circular dichroism studies reveal that the helical content of bovine serum albumin decreased after interaction with naringin. According to the F?rster non-radiative energy transfer theory the distance between Trp 213 residue and naringin was found to be 3.25 nm. Displacement studies suggest that naringin binds to site 1 (subdomain IIA) of bovine serum albumin (BSA) which was also substantiated by molecular docking studies.

"Doubling" of local photon emissions when two simultaneous, spatially-separated, chemiluminescent reactions share the same magnetic field configurations

Abstract: The aim of the present experiments was to discern if the “entanglement”-like photon emissions from pairs of cell cultures or human brains separated by significant distances but sharing the same circling magnetic field could be demonstrated with a classic chemiluminescent reaction produced by hydrogen peroxide and hypochlorite. Simultaneous injection of the same amount of peroxide into a local dish (above a photomultiplier tube) and a dish 10 m away in a closed chamber produced a “doubling” of the durations of the photon spikes only when the two reactions were placed in the center of separate spaces around each of which magnetic fields were generated as accelerating group velocities containing decreasing phase modulations followed by decelerating group velocities embedded with increasing phase modulations. The duration of this “entanglement” was about 8 min. These results suggest that separate distances behave as if they were “the same space” if they are exposed to the same precise temporal configuration of magnetic fields with specific angular velocities.

Thermodynamic solvation of a series of homologous α-amino acids in non-aqueous mixture of ethylene-glycol and N,N-dimethyl formamide

Abstract: Standard free energies (ΔG0t(i) ) and entropies (ΔS0t(i)) of transfer of some homologous α-amino acids viz. glycine (gly), dl-alanine (ala), dl-α-amino butyric acid (aba) and dl-nor-valine (nor-val) from protic ethylene glycol (EG) to dipolar aprotic N,N-dimethyl formamide (DMF) have been evaluated from solubility measure-ments at five equidistant temperatures i.e from 15 to 350C. The observed ΔG0t(i) and TΔS0t(i) Vs composition profiles are complicated because of the various interaction effects. The chemical effects of the transfer Gibbs energies (ΔG0t.ch(i)) and entropies of transfer (ΔS0t.ch(i)) have been obtained after elimination of cavity effect, estimated by the scaled particle theory and dipole-dipole interaction effects, estimated by the use of Keesom-orientation expression. The chemical contributions of transfer energetics of homologous α-amino acids are guided by the composite effects of increased dispersion interaction, basicity and decreased acidity, hydrogen bonding effects and solvophobic solvation of ethylene glycol and N, N-dimethyl formamide mixed solvent as compared to that of reference solvent (ethylene glycol).