Abstract
Melittin is a small amphipathic cationic membrane-active protein in bee venom. Apart from being a key agent in envenomation, melittin is a physiologically active protein with important pharmacological properties that include anti-cancer and antimicrobial activities. Perhaps melittin's most important property is its ability to modulate the activity of endogenous phospholipase A2 (PLA<sub>2</sub>) both <em>in vivo</em> and <em>in vitro</em>.
Highlights
Bee venom melittin is an amphipathic cationic membrane-active polypeptide of 26 amino acid residues [1]
In this study we have used a lipid to melittin molar ratio 100 to 1 as we wanted to investigate the effects of melittin on the PC membrane packing order and on phospholipase A2 (PLA2) esterase activity at a threshold at which a disturbed PC bilayer packing starts changing to a nonlamellar PC formation of stable pores
The results of this study strongly suggest for the first time that the melittin association with PLA2 enzymes in solution is driven by the forces of electrostatic attraction but not by the hydrophobic forces of attraction
Summary
Bee venom melittin is an amphipathic cationic membrane-active polypeptide of 26 amino acid residues [1]. When melittin binds to membrane surfaces it induces changes in the membrane structural integrity including formation of pores, formation of vesicles and fusion of membranes [6,7]. These changes in membrane structure promote changes in membrane potential [8], in aggregation of membrane proteins [9], and in induction of hormone secretion [10]. The molecular mechanisms underlying the diverse effects of melittin are not fully understood
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