Deciphering the Kinetic Study of Sodium Dodecyl Sulfate on Ag Nanoparticle Synthesis Using Cassia siamea Flower Extract as a Reducing Agent.

Silver nanoparticles (Ag NPs) were synthesized using Cassia siamea flower petal extract (CSFE) as a reducing agent for the first time. In its presence and absence, the correlative effects of the anionic surface-active agent sodium dodecyl sulfate (SDS) were studied with respect to the development and texture of Ag NPs. Under different reagent compositions, the Ag NPs were inferred by localized surface plasmon resonance peaks between 419 and 455 nm. In the absence of SDS, there was a small eminence at 290 and around 350 nm, pointing toward the possibility of irregular polytope Ag NPs, which was confirmed in the transmission electron microscopy images. This elevation vanished beyond the cmc of [SDS], resulting in spherical and oval shaped Ag NPs. The effects of reagent concentrations were studied at 25 °C and around 7 and 9 pH in the absence and presence of SDS, respectively. Also, kinetic studies were performed by UV-visible spectrophotometry. Prodigious effects on shape and size were found under different synthesis conditions in terms of hexagonal, rod-, irregular-, and spherical shaped Ag NPs. Furthermore, the antimycotic activity of the synthesized Ag NPs was established on different Candida strains, and best results were found pertaining Candida tropicalis. The ensuing study impels the control of texture and dispersity for Ag NPs by CSFE and SDS, and the resultant polytope Ag NPs could be a future solution for drug-resistant pathogenic fungi.

Hydrogen bonding-assisted interaction between amitriptyline hydrochloride and hemoglobin: spectroscopic and molecular dynamics studies.

Herein, we have explored the interaction between amitriptyline hydrochloride (AMT) and hemoglobin (Hb), using steady-state and time-resolved fluorescence spectroscopy, UV-visible spectroscopy, and circular dichroism spectroscopy, in combination with molecular docking and molecular dynamic (MD) simulation methods. The steady-state fluorescence reveals the static quenching mechanism in the interaction system, which was further confirmed by UV-visible and time-resolved fluorescence spectroscopy. The binding constant, number of binding sites, and thermodynamic parameters viz. ΔG, ΔH, ΔS are also considered; result confirms that the binding of the AMT with Hb is a spontaneous process, involving hydrogen bonding and van der Waals interactions with a single binding site, as also confirmed by molecular docking study. Synchronous fluorescence, CD data, and MD simulation results contribute toward understanding the effect of AMT on Hb to interpret the conformational change in Hb upon binding in aqueous solution.

Refolding of urea denatured cytochrome c: Role of hydrophobic tail of the cationic gemini surfactants.

The refolding of urea denatured horse heart cytochrome c (h-cyt-c) under the influence of ester based cationic gemini surfactants [ethane-1, 2-diyl bis(N, N-dimethyl-N-alkylammoniumacetoxy) dichlorides] 16-E2-16, 14-E2-14 and 12-E2-12 (n-E2-n) was performed by using UV-visible, fluorescence and circular dichroism (CD) spectroscopic techniques. We found that n-E2-n geminis promote the formation of molten globule (MG) like state upon addition into the urea denatured h-cyt-c. The comparative study of refolding of denatured h-cyt-c with n-E2-n, cationic gemini surfactant show stabilization of MG-like state influenced by hydrophobic interactions. The formation of MG-like state from the unfolded protein confirms the presence of some regular structures induced by n-E2-n gemini surfactants. Thermodynamic parameters for refolding of h-cyt-c by n-E2-n were also measured and the m-values of all the refolded states of h-cyt-c by n-E2-n show marked difference. The higher m-values correspond to the larger hydrophobic chain length indicates that refolding ability of the n-E2-n depends on the alkyl chain length. The result is related to the stronger hydrophobic forces due to the presence of two head groups and two hydrophobic hydrocarbon tails. This study showed that these cationic gemini surfactants were efficiently utilized in the protein refolding studies.

Urea-induced binding between diclofenac sodium and bovine serum albumin: a spectroscopic insight.

We investigated the interaction of diclofenac sodium (Dic.Na) with bovine serum albumin (BSA) in the absence and presence of urea using different spectroscopic techniques. A fluorescence quenching study revealed that the Stern-Volmer quenching constant decreases in the presence of urea, decreasing further at higher urea concentrations. The binding constant and number of binding sites were also evaluated for the BSA-Dic.Na interaction system in the absence and presence of urea using a modified Stern-Volmer equation. The binding constant is greater at high urea concentrations, as shown by the fluorescence results. In addition, for the BSA-Dic.Na interaction system, a static quenching mechanism was observed, which was further confirmed using time-resolved fluorescence spectroscopy. UV-vis spectroscopy provided information about the formation of a complex between BSA and Dic.Na. Circular dichroism was carried out to explain the conformational changes in BSA induced by Dic.Na in the absence and presence of urea. The presence of urea reduced the α-helical content of BSA as the Dic.Na concentration varied. The distance r between the donor (BSA) and acceptor (Dic.Na) was also obtained in the absence and presence of urea, using fluorescence resonance energy transfer. Copyright © 2015 John Wiley & Sons, Ltd.

Spectroscopic and molecular modelling analysis of the interaction between ethane-1,2-diyl bis(N,N-dimethyl-N-hexadecylammoniumacetoxy)dichloride and bovine serum albumin.

Several spectroscopic approaches namely fluorescence, time-resolved fluorescence, UV-visible, and Fourier transform infra-red (FT-IR) spectroscopy were employed to examine the interaction between ethane-1,2-diyl bis(N,N-dimethyl-N-hexadecylammoniumacetoxy)dichloride (16-E2-16) and bovine serum albumin (BSA). Fluorescence studies revealed that 16-E2-16 quenched the BSA fluorescence through a static quenching mechanism, which was further confirmed by UV-visible and time-resolved fluorescence spectroscopy. In addition, the binding constant and the number of binding sites were also calculated. The thermodynamic parameters at different temperatures (298 K, 303 K, 308 K and 313 K) indicated that 16-E2-16 binding to BSA is entropy driven and that the major driving forces are electrostatic interactions. Decrease of the α-helix from 53.90 to 46.20% with an increase in random structure from 22.56 to 30.61% were also observed by FT-IR. Furthermore, the molecular docking results revealed that 16-E2-16 binds predominantly by electrostatic and hydrophobic forces to some residues in the BSA sub-domains IIA and IIIA.

Recent advances in the applications of ionic liquids in protein stability and activity: a review.

Room temperatures ionic liquids are considered as miraculous solvents for biological system. Due to their inimitable properties and large variety of applications, they have been widely used in enzyme catalysis and protein stability and separation. The related information present in the current review is helpful to the researchers working in the field of biotechnology and biochemistry to design or choose an ionic liquid that can serve as a noble and selective solvent for any particular enzymatic reaction, protein preservation and other protein based applications. We have extensively analyzed the methods used for studying the protein-IL interaction which is useful in providing information about structural and conformational dynamics of protein. This can be helpful to develop and understanding about the effect of ionic liquids on stability and activity of proteins. In addition, the affect of physico-chemical properties of ionic liquids, viz. hydrogen bond capacity and hydrophobicity on protein stability are discussed.

Spectroscopic and docking studies on the interaction between pyrrolidinium based ionic liquid and bovine serum albumin.

The interaction of synthesized ionic liquid, 1-butyl-1-methyl-2-oxopyrrolidinium bromide (BMOP) and bovine serum albumin (BSA) was investigated using UV-Vis, FT-IR, steady state and time resolved fluorescence measurements and docking studies. Steady state spectra revealed that BMOP strongly quenched the intrinsic fluorescence of BSA through dynamic quenching mechanism. The corresponding thermodynamic parameters; Gibbs free energy change (ΔG), entropy change (ΔS) and enthalpy change (ΔH) showed that the binding process was spontaneous and entropy driven. It is also indicated that hydrophobic forces play a key role in the binding of BMOP to BSA. The synchronous fluorescence spectroscopy reveals that the conformation of BSA changed in the presence of BMOP. The shift in amide I band of FT-IR spectrum of BSA suggested unfolding of the protein secondary structure upon the addition of BMOP. In addition, the molecular modeling study of BSA-BMOP system shows that BMOP binds with BSA at the interface between two sub domains IIA and IIIA, which is located just above the entrance of the binding pocket of IIA through hydrophobic and hydrogen bond interactions in which hydrophobic interaction are dominated.

Role of 1-methyl-3-octylimidazolium chloride in the micellization behavior of amphiphilic drug amitriptyline hydrochloride.

The mixed micellization behaviour of amitriptyline hydrochloride (AMT) with ionic liquid (IL) 1-methyl-3-octylimidazolium hydrochloride, [C8mim][Cl], have been investigated using electrical conductivity, at different temperatures. The non-ideal behaviour (i.e., synergistic interaction) of AMT-[C8mim][Cl] binary mixtures, explained by the deviations in critical micelle concentration (cmc) from ideal critical micelle concentration (cmc*) and micellar mole fraction (X(m)) from ideal micellar mole fraction (X(ideal)) values. The values of interaction parameter (ß) and activity coefficients (f1 and f2), also confirm the synergistic interaction. The excess free energy (ΔGex) for the AMT-[C8mim][Cl] binary mixtures explains, stability of mixed micelles in comparison to micelles of pure, AMT and [C8mim][Cl]. The calculated thermodynamic parameters (viz., the standard Gibbs energy change, ΔGm(∘), the standard enthalpy change, ΔHm(∘), the standard entropy change, ΔSm(∘)), suggest the dehydration of hydrophobic part of the drug at higher temperatures (>313K), not only in case of AMT but also in the presence of [C8mim][Cl].

Interaction of amphiphilic drugs with human and bovine serum albumins.

To know the interaction of amphiphilic drugs nortriptyline hydrochloride (NOT) and promazine hydrochloride (PMZ) with serum albumins (i.e., human serum albumin (HSA) and bovine serum albumin (BSA)), techniques of UV-visible, fluorescence, and circular dichroism (CD) spectroscopies are used. The binding affinity is more in case of PMZ with both the serum albumins. The quenching rate constant (k(q)) values suggest a static quenching process for all the drug-serum albumin interactions. The UV-visible results show that the change in protein conformation of PMZ-serum albumin interactions are more prominent as compared to NOT-serum albumin interactions. The CD results also explain the conformational changes in the serum albumins on binding with the drugs. The increment in %α-helical structure is slightly more for drug-BSA complexes as compared to drug-HSA complexes.

Effect of ionic liquid on activity, stability, and structure of enzymes: a review.

Ionic liquids have shown their potential as a solvent media for many enzymatic reactions as well as protein preservation, because of their unusual characteristics. It is also observed that change in cation or anion alters the physiochemical properties of the ionic liquids, which in turn influence the enzymatic reactions by altering the structure, activity, enatioselectivity, and stability of the enzymes. Thus, it is utmost need of the researchers to have full understanding of these influences created by ionic liquids before choosing or developing an ionic liquid to serve as solvent media for enzymatic reaction or protein preservation. So, in the present review, we try to shed light on effects of ionic liquids chemistry on structure, stability, and activity of enzymes, which will be helpful for the researchers in various biocatalytic applications.

Spectroscopic approach of the interaction study of amphiphilic drugs with the serum albumins.

The interaction of the amphiphilic drugs, i.e., amitriptyline hydrochloride (AMT) and promethazine hydrochloride (PMT), with serum albumins (i.e., human serum albumin (HSA) and bovine serum albumin (BSA)), has been examined by the various spectroscopic techniques, like fluorescence, UV-vis, and circular dichroism (CD). Fluorescence results indicate that in case of HSA-drug complexes the quenching of fluorescence intensity at 280 nm is less effective as compared to at 295 nm while in case of BSA-drug complexes both have almost same effect and for most of drug-serum albumin complexes there is only one independent class of binding. For all drug-serum albumin complexes the quenching rate constant (K(q)) values suggest the static quenching procedure. The UV-vis results show that the change in protein conformation of PMT-serum albumin complexes was more prominent as compared to AMT-serum albumin complexes. The CD results also explain the conformational changes in the serum albumins on binding with drugs. The increase in α-helical structure for AMT-serum albumin complexes is found to be more as compared to PMT-serum albumin complexes. Hence, the various spectroscopic techniques provide a quantitative understanding of the binding of amphiphilic drugs with serum albumins.

Mixed micellization of antidepressant drug amitriptyline hydrochloride with cationic surfactants.

The surface tension measurements have been carried out on aqueous solutions of antidepressant drug amitriptyline hydrochloride with six cationic surfactants (decyl-, dodecyl-, tetradecyl-, cetyltrimethylammonium bromide, cetylpyridinium bromide and cetylpyridinium chloride) at different mole fractions to study the surface and micellar properties at the interface as well as in the micelles. The properties studied include critical micelle concentration (cmc), Gibbs surface excess (Gamma(max)), minimum head group area at the air/water interface (A(min)), free energy of micellization (DeltaG(m)( composite function)), and standard Gibbs energy of adsorption (DeltaG(ads)( composite function)), while synergistic behavior of drug-surfactant binary mixtures was analysed using Clint's and Rubingh's models. Deviations of cmc from cmc(*) and X(1)(m) from X(1)(ideal) indicate the synergistic behavior (i.e., non-ideal behavior) for the drug-surfactant binary mixtures. The values of interaction parameters beta and activity coefficients f(1) and f(2) (for both, in mixed monolayer as well as in mixed micelles) also indicate the synergistic behavior. The excess free energy (DeltaG(ex)) for the drug-surfactant binary mixtures explains stability of mixed micelles in comparison to micelles of pure drug and variation with alkyl chain length of surfactants.