Pore formation of phospholipid membranes by the action of two hemolytic arachnid peptides of different size.
Pin2 and Oxki1 are cationic amphipathic peptides that permeate lipid membranes through formation of pores. Their mechanism of binding to phosphocholine (PC) membranes differs. Spin-probe experiments showed that both Pin2 and Oxki1 penetrate the lipid membrane of small unilamellar vesicles (SUVs). Moreover, the leakage of calcein and dextrans from PC vesicles showed that Pin2 agrees with the accumulation of peptides on lipid membranes and form pores of different size. On the other hand, Oxki1 did not act strictly cooperatively and form pores of limited size.
Suntory Institute for Bioorganic Research, 1-1-1 Wakayamadai, Shimamoto-cho, Mishima-gun, Osaka 618-8503, Japan.
Olga S
OS
Belokoneva
Honoo
H
Satake
Elena L
EL
Mal'tseva
Nadezhda P
NP
Pal'mina
Elba
E
Villegas
Terumi
T
Nakajima
Gerardo
G
Corzo
D000595:Amino Acid Sequence; D006461:Hemolysis; D008081:Liposomes; D008563:Membrane Lipids / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000494:pharmacology*; D010539:Permeability; D010743:Phospholipids / Q000378:metabolism*; D012604:Scorpion Venoms / Q000494:pharmacology*
D008081:Liposomes; D008563:Membrane Lipids; D010455:Peptides; D010743:Phospholipids; D012604:Scorpion Venoms; C476118:pandinin 2