Transition from antagonistic to synergistic interaction in mixed micellar system by increase in alkyl chain length of alkyl trimethylammonium bromide

Herein, the electrical conductivity technique used to measure the critical micelle concentration (cmc) for pure cationic surfactants (Dodecyl/cetyltrimethylammonium bromides) and phenothiazine drug (Promethazine hydrochloride), as well as their different mole fractions in 10^?3 ?mol/kg 1-methyl-3-octylimidazolium chloride (C₈mim.Cl) at different temperatures. By using the cmc values the regular solution theory used to evaluate the micellar mole fraction for DTAB/CTAB-PMT mixed systems. The clint's model used to calculate the ideal critical micelle concentration (cmc1) that helps to evaluate the ideal micellar mole fraction for studied mixed systems, both explain the deviation from ideality. In addition, interaction parameter β^m helps to confirm the nature of interaction (either antagonistic or synergistic) for the studied systems. The calculated parameters confirm a transition in the binding nature from antagonistic to synergistic with the increase in alkyl chain length of cationic surfactant i.e., component of the binary mixed system. The ease of micellization for the studied systems discussed by the standard Gibb's energy of micellization ($\Delta G_m^0$), as well as the standard enthalpy and standard entropy of micellization were ($\Delta H_m^0$) and ($\Delta S_m^0$), respectively to discuss the stability of the studied systems.     

Isolation and Characterization of Cross-Neutralizing Human Anti-V3 Single-Chain Variable Fragments (scFvs) Against HIV-1 from an Antigen Preselected Phage Library

Applied Biochemistry and Biotechnology - Recently conducted human phase- I trials showed protective effect of anti-HIV-1 broadly neutralizing antibodies (bnAbs). The V3 region of the HIV-1 envelope...     

Elucidating the Role of Santalol as a Potent Inhibitor of Tyrosinase: In Vitro and In Silico Approaches

This research work focuses on the potential application of an organic compound, santalol, obtained from santalum album, in the inhibition of the enzyme tyrosinase, which is actively involved in the biosynthesis of melanin pigment. Over-production of melanin causes undesirable pigmentation in humans as well as other organisms and significantly downgrades their aesthetic value. The study is designed to explain the purification of tyrosinase from the mushroom Agaricus bisporus, followed by activity assays and enzyme kinetics to give insight into the santalol-modulated tyrosinase inhibition in a dose-dependent manner. The multi-spectroscopic techniques such as UV-vis, fluorescence, and isothermal calorimetry are employed to deduce the efficiency of santalol as a potential candidate against tyrosinase enzyme activity. Experimental results are further verified by molecular docking. Santalol, derived from the essential oils of santalum album, has been widely used as a remedy for skin disorders and a potion for a fair complexion since ancient times. Based on enzyme kinetics and biophysical characterization, this is the first scientific evidence where santalol inhibits tyrosinase, and santalol may be employed in the agriculture, food, and cosmetic industries to prevent excess melanin formation or browning.     

Structural Refolding and Thermal Stability of Myoglobin in the Presence of Mixture of Crowders: Importance of Various Interactions for Protein Stabilization in Crowded Conditions

The intracellular environment is overcrowded with a range of molecules (small and large), all of which influence protein conformation. As a result, understanding how proteins fold and stay functional in such crowded conditions is essential. Several in vitro experiments have looked into the effects of macromolecular crowding on different proteins. However, there are hardly any reports regarding small molecular crowders used alone and in mixtures to observe their effects on the structure and stability of the proteins, which mimics of the cellular conditions. Here we investigate the effect of different mixtures of crowders, ethylene glycol (EG) and its polymer polyethylene glycol (PEG 400 Da) on the structural and thermal stability of myoglobin (Mb). Our results show that monomer (EG) has no significant effect on the structure of Mb, while the polymer disrupts its structure and decreases its stability. Conversely, the additive effect of crowders showed structural refolding of the protein to some extent. Moreover, the calorimetric binding studies of the protein showed very weak interactions with the mixture of crowders. Usually, we can assume that soft interactions induce structural perturbations while exclusion volume effects stabilize the protein structure; therefore, we hypothesize that under in vivo crowded conditions, both phenomena occur and maintain the stability and function of proteins.