Reference : Thermodynamic Studies Of The Binding Interactions Of Surfactin Analogues To Lipid Vesicl...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/16415
Thermodynamic Studies Of The Binding Interactions Of Surfactin Analogues To Lipid Vesicles Application Of Isothermal Titration Calorimetry
English
Razafindralambo, Hary mailto [Université de Liège - ULg > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech >]
Dufour, Samuel [> >]
Paquot, Michel [Université de Liège > > Gembloux Agro-Bio Tech >]
Deleu, Magali [Université de Liège > > Gembloux Agro-Bio Tech >]
2009
Journal of Thermal Analysis and Calorimetry
Springer
95
3
817-821
Yes (verified by ORBi)
International
1388-6150
Dodrecht
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.
Researchers ; Professionals ; Students ; General public ; Others
http://hdl.handle.net/2268/16415
10.1007/s10973-008-9403-6

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