Effect of Cationic Amphiphiles and Temperature on Lysozyme Conformation

Ericsson, Bodil; Hegg, Per‐Olof; Mårtensson, Kaj

doi:10.1080/01932698708943607

Cited by 5 publications

(4 citation statements)

References 25 publications

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“…This difference in behavior between anionic and cationic surfactants with respect to their micellization in a gelatin solution is further suggested to be due to the contribution arising from relatively stronger hydrophobic interactions between protein and surfactant molecules especially in view of the fact that the hydrophobic part carried by different positively charged amino acid residues is longer than that of negatively charged amino acid residues [17,18]. This data thus tend to show that the screening of a positive charge of a polar head group of CTAB, CTAC, and DDAB is likely to be the cause of such behavior.…”

Section: Resultsmentioning

confidence: 94%

Sound Speed and Density Studies of Interactions Between Cationic Surfactants and Aqueous Gelatin Solution

Chauhan

et al. 2012

Int J Thermophys

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Studies on the interactions of surfactants with proteins can contribute to an understanding of the action of surfactants as denaturants and as solubilizing agents for membranes of proteins and lipids. Quantitative aspects of such studies may include direct measurements of properties, such as viscosity, density, sound speed, conductance, and elucidation of the often highly complex phase diagrams. In this study, sound speed and density studies of surfactants, viz., cetyltrimethyl ammonium bromide, cetyltrimethyl ammonium chloride, and di(dodecydimethyl ammonium bromide) (12-2-12) have been carried out in a 0.02 % w/v aqueous solution of gelatin at temperatures of 20 • C, 25 • C, 30 • C, and 35 • C. From the measured data, the parameters apparent molar volumes (φ v ), adiabatic compressibility (β), and apparent molar compressibility (φ k ) have been calculated to interpret the protein-surfactant interactions. The variations in these parameters with the concentration of the surfactant suggests the manifestation of hydrophobic interactions in the system.

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Section: Resultsmentioning

confidence: 94%

Sound Speed and Density Studies of Interactions Between Cationic Surfactants and Aqueous Gelatin Solution

Chauhan

et al. 2012

Int J Thermophys

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“…The second plateau observed in surface tension isotherms for ovalbumin and HPC mixtures just below cmc of HPC ( Fig. 5.17c), can be related to the electrostatic interaction between HPC and globular proteins that has been observed below cmc in bulk solution (Ericsson et al, 1987a). It is noteworthy that the surface tension is slightly lower than for pure HPC, suggesting that the complex is more surface active.…”

Section: Fig 517amentioning

confidence: 82%

“…Although cationic surfactants seem to cause less unfolding of globular proteins at low temperature than anionic, some reports indicate that they can destabilize globular proteins at increased temperature (Ericsson et al, 1983a;Ericsson et al, 1987a). However, these reports also indicate that the unfolding process at the same time becomes considerably more reversible.…”

Section: Effect Of Solution Conditionsmentioning

confidence: 99%

“…Reports in the literature indicate a cooperative interaction with proteins, but with less affinity and thus with less perturbation of the folded state, compared to the effect of the anionic ones (Tanford and Epstein, 1954;Kaneshina et al, 1973;Nozaki et al, 1974;Ericsson et al, 1987a;Ericsson et al, 1987b;Waninge et al, 1998). If the binding is governed both by electrostatic and hydrophobic interactions, anionic and cationic surfactants will obviously occupy different sites.…”

Section: Cationicmentioning

confidence: 99%

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