A region-matched hydrophobic interaction between melittin and dimyristoylphosphatidylcholine in a ternary mixture of phosphatidylcholines.
Interaction of melittin with phosphatidylcholine molecules in pure vesicles, binary mixtures and a ternary mixture of dimyristoylphosphatidylcholine IDMPC), dipalmitoylphosphatidylcholine (DPPC) and distearoylphosphatidylcholine (DSPC) was investigated by differential scanning calorimetry. Melittin binds preferentially with DMPC, and results in segregation of DMPC in binary mixtures of DMPC/DPPC and DMPC/DSPC and in a ternary mixture of DMPC/DPPC/DSPC. The results indicate that the hydrophobic part of peptide interacts preferentially with the phospholipid which has the same size of hydrophobic region or fatty acyl chains.
Ohki
K
K
Department of Applied Physics, School of Engineering, Nagoya University, Japan.
D015060:1,2-Dipalmitoylphosphatidylcholine; D001514:Bee Venoms; D002152:Calorimetry, Differential Scanning; D004134:Dimyristoylphosphatidylcholine; D008051:Lipid Bilayers; D008555:Melitten; D008954:Models, Biological; D010713:Phosphatidylcholines; D011485:Protein Binding
D001514:Bee Venoms; D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D008555:Melitten; D015060:1,2-Dipalmitoylphosphatidylcholine; C010942:1,2-distearoyllecithin; D004134:Dimyristoylphosphatidylcholine