Thermodynamic studies of the binding interactions of surfactin analogues to lipid vesicles

Application of isothermal titration calorimetry
  • H. Razafindralambo
  • S. Dufour
  • M. Paquot
  • M. Deleu


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 10mMTris buffer at pH8.5with 150mMNaCl at 25°C. Surfactin analogues interacted spontaneously (ΔG D w→b < 0) with POPC vesicles. The binding reactions were endothermic (ΔH D w→b > 0) and entropy-driven process (ΔS D w→b > 0). Moreover, significant differences in the binding constant values (K) ranging from 6.6·103 to 9.6·104 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.


interaction isothermal titration calorimetry lipid vesicles lipopeptide surfactin 


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Copyright information

© Akadémiai Kiadó, Budapest, Hungary 2009

Authors and Affiliations

  • H. Razafindralambo
    • 1
  • S. Dufour
    • 1
  • M. Paquot
    • 1
  • M. Deleu
    • 1
  1. 1.Unité de Chimie Biologique IndustrielleFaculté Universitaire des Sciences Agronomiques de GemblouxGemblouxBelgium

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