Accueil > Publications > Recherche par années > Années 1990 > 1995

Faucon, JF ; Bonmatin, JM ; Dufourcq, J ; Dufourc, EJ

Acyl-chain length dependence in the stability of melittin-phosphatidylcholine complexes - a light-scattering and p-31-NMR study

Biochimica et Biophysica Acta-Biomembranes 1234 (2) 235-243

par Administrateur - publié le

Abstract :

Light scattering and P-31-NMR have been used to monitor the effect of the bee-toxin, melittin, on phosphatidylcholine (PC) bilayers of variable acyl chain length (from C-16:0 to C-20:0). Melittin interacts with all lipids provided the interaction is initiated in the lipid fluid phase. For low-to-moderate amounts of toxin (lipid-peptide molar ratios, R(i) greater than or equal to 15), the system takes the form of large spheroidal vesicles, in the fluid phase, whose radius increases from 750 Angstrom A with dipalmitoyl-PC (DPPC) to 1500 Angstrom A with diarachinoyl-PC (DAPC). These vesicles fragment into small discoids of 100-150 Angstrom A radius when the system is cooled down below T-c (the gel-to-fluid phase transition temperature).