Physicochemical studies of globular proteins—Bovine serum albumin, egg albumin, and lysozyme—In some aqueous iodide salts solutions of IA group and cetyltrimethyl ammonium bromide systems

Singh, Man

doi:10.1002/app.26733

Cited by 3 publications

(1 citation statement)

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“…In drug delivery, − cosmetic formulation (with special reference to body and skin care products), − nanomaterial preparation, − pharmaceutical and industrial fields, − etc., polymer−surfactant (or lipid) interaction is involved in one way or another. Water-soluble synthetic and modified polymers, viz., polyethylene oxide, − polyethyleneglycols, , polyvinylpyrrolidone (PVP), − carboxymethyl cellulose, − the N , N -dimethyl- N -methyl derivative of hydroxyethylcellulose (JR 400), , the N , N -dimethyl- N -dodecyl derivative of hydroxyethylcellulose (LM 200), , etc., carbohydrate polymers, viz., starch, − amylose, − amylopectin, − etc., and proteins, viz., bovine serum albumin, − lysozyme, − gelatin, − hemoglobin, , pepsin, papain, − egg albumin, etc., have been amply used for their interaction with different amphiphiles. The strength of binding, changes in the configuration of the polymers upon interaction, types of products formed, their evolved physicochemical properties, etc.…”

Section: Introductionmentioning

confidence: 99%

Physicochemistry of the Interaction between Inulin and Alkyltrimethylammonium Bromides in Aqueous Medium and the Formed Coacervates

2009

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Inulin, a polydisperse reserve polysaccharide, has prospective uses in food, pharmacy, and industry. Its uses and applications often encounter interactions with lipids and amphiphiles. Reports on such interactions are scarcely found in literature. In the present study, we have examined the nature of interactions between inulin and cationic amphiphiles, alkyltrimethylammonium bromides (CnTAB: n=12, 14, 16, 18), over a fair range of concentrations for both the polymer and the amphiphile. At low concentration, small induced amphiphile aggregates form complexes with inulin; at moderate concentration, the complexed inulin self-aggregates leading to coacervate formation, and at higher concentration, the amphiphile forms free micelles in solution. Tensiometric, conductometric, viscometric, and turbidimetric methods have been employed to study the above phenomena. The isolated coacervates of inulin with C18TAB were examined by scanning electron microscopy (SEM), transmission electron microscopy (TEM), atomic force microscopy (AFM), differential scanning calorimetry (DSC), thermogravimetry (TG), and differential thermal analysis (DTA) to ascertain their morphology, structure, and thermal stability.

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Section: Introductionmentioning

confidence: 99%

Physicochemistry of the Interaction between Inulin and Alkyltrimethylammonium Bromides in Aqueous Medium and the Formed Coacervates

2009

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Characterization of BSA unfolding and aggregation using a single-capillary viscometer and dynamic surface tension detector

Bramanti

Ferrari

Angeli

et al. 2011

Talanta

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Comparative study of ionic interactions of 1 : 1 and 1 : 2 electrolytes of nitrates salts solutions with water analysed with physicochemical data

Mukherjee

Singh

Bhanumati

2012

Physics and Chemistry of Liquids

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Densities (), viscosities () and surface tension () as function of the molarity of 0.1, 0.2, 0.3, 0.4, 0.5 and 0.6 for LiNO 3 , NaNO 3 , KNO 3 , Sr(NO 3 ) 2 , Ba(NO 3 ) 2 and Pb(NO 3 ) 2 electrolytes are reported at 32 C. Data were regressed for limiting values for solute-solvent interactions and effects of shell numbers and electronic configurations. A confidence variance of 95.5% at Gaussian distribution was noted. Densities explained ionic forces and sizes, and viscosities defined frictional forces while the surface tension focused surface energies of hydrated ions. Slopes of densities, viscosities and surface tensions explained the concentration effects on ionic interactions. Limiting densities from Li þ to Ba 2þ increased with increase in sizes. Pb 2þ smaller in size than the Ba 2þ had lower limiting densities. The 0 are Ba 2þ > Sr 2þ > Pb 2þ > K þ > Na þ > Li þ with 3.24, 2.98, 4.53, 2.109, 2.257 and 2.38 Â 10 3 kg m À3 densities of nitrate salts, respectively, in the solid state.

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Physicochemical studies of globular proteins—Bovine serum albumin, egg albumin, and lysozyme—In some aqueous iodide salts solutions of IA group and cetyltrimethyl ammonium bromide systems

Cited by 3 publications

References 46 publications

Physicochemistry of the Interaction between Inulin and Alkyltrimethylammonium Bromides in Aqueous Medium and the Formed Coacervates

Physicochemistry of the Interaction between Inulin and Alkyltrimethylammonium Bromides in Aqueous Medium and the Formed Coacervates

Characterization of BSA unfolding and aggregation using a single-capillary viscometer and dynamic surface tension detector

Comparative study of ionic interactions of 1 : 1 and 1 : 2 electrolytes of nitrates salts solutions with water analysed with physicochemical data

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