Interaction of biocompatible sugar based surfactant n-dodecyl β-d-maltoside with lysozyme

The industrial anaerobe Clostridium acetobutylicum uses polyketides to regulate cellular differentiation

“…This behavior suggested that one or more of the polyketides might act as surfactants to permit colony spreading over the agar surface, as self-produced surfactants are known to permit surface motility in some microbes 36 . To test this, we performed standard assays for surfactant activity (oil spreading and drop collapse assays) using pure clostrienose ( 3 ), given that this compound displays some structural similarities to known non-ionic surfactants such as n -dodecyl-β- d -maltosides 37 and rhamnolipids 38 . As shown in Supplementary Tables 3 and 4 , clostrienose displayed weak surfactant activity at relatively high concentrations (100 µM), but little to no surfactant activity near physiological concentrations (10 µM) according to the oil spreading assay.…”

Insights into the Interactions of Sulfamethoxazole with Organized Assemblies of Ionic and Nonionic Surfactants

“…The cmc of the surfactant in the presence of SMX shifted toward a higher concentration (1.8 × 10 –3 mol dm –3 ), which is an indication of the utilization of surfactant monomers in binding with SMX, which leads to delayed micellization. The slope of the tensiometric profile near the cmc is a measure of interfacial adsorption efficacy of the surfactant, which was quantified by the Gibbs surface excess (γ max ) − and is given by where γ is the surface tension of the solution, R is the universal gas constant (8.314 J K –1 mol –1 ), T is the temperature in the absolute scale, C is the concentration of the surfactant in solution, and n is a constant that depends on the number of species constituting the surfactant, and in the present case, it is equal to 1 because of the presence of high ionic strength of the buffer solution used. The minimum area of exclusion per molecule at the saturated air/solution interface ( A min ) is given by where N A is Avogadro’s number.…”

Interaction of the lysozyme with anticoagulant drug warfarin: Spectroscopic and computational analyses

“…Therefore, we have selected lysozyme protein to see its interaction with warfarin and also to understand its potential as a carrier because it can bind a lot of molecules in its large cavity [ [36] , [37] , [38] , [39] , [40] , [41] , [42] ]. Additionally, the effect of warfarin on the structure of the protein which also occurs inside human body was also a topic of concern.…”