Reference : Thermodynamic Studies Of The Binding Interactions Of Surfactin Analogues To Lipid Ves...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Thermodynamic Studies Of The Binding Interactions Of Surfactin Analogues To Lipid Vesicles Application Of Isothermal Titration Calorimetry
Razafindralambo, Hary [Université de Liège - ULiège > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech >]
Dufour, Samuel [> >]
Paquot, Michel [Université de Liège - ULiège > > Gembloux Agro-Bio Tech >]
Deleu, Magali [Université de Liège - ULiège > > Gembloux Agro-Bio Tech >]
Journal of Thermal Analysis and Calorimetry
Yes (verified by ORBi)
The Netherlands
[en] interaction; isothermal titration calorimetry; lipid vesicles, lipopeptide, surfactin
[en] Isothermal titration calorimetry was applied for studying the binding interactions of cyclic and linear surfactins with different ionic charge (z= –2 and –3) and lipid chain length (n=14 and 18) to 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidyl-choline (POPC) vesicles in 10mM Tris buffer at pH 8.5 with 150mM NaCl at 25°C. Surfactin analogues interacted spontaneously with POPC vesicles. The binding reactions were endothermic and entropy-driven process. Moreover, significant differences in the binding constant values (K) ranging from 6.6 *10^3 to 9.6* 10^4 M–1 show that cyclic structure and the increase of lipid chain length are favourable on the surfactin binding affinity to POPC vesicles, whereas the rise of the number of negative charges has an opposite effect.
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