Abstract
Cobra phospholipase A2, a α-helix acidic polypeptide, is known to hydrolyze membrane and involve some cell signaling pathways. Herein, we demonstrate that the major cobra phospholipase A2 ( Naja atra ), By the combined polarized attenuated total reflection infrared spectroscopy and computer simulation studies, Naja atra phospholipase A2 is shown to peripherally bind to multilayers in a similar edgewise manner with a tilted angle of 160° between theα-helix plane of the Cobra phospholipase A2 molecule and the normal of the membrane surface. Qualitatively speaking, theα-helix plane of the Cobra phospholipase A2 molecule with (90°,60°) orientation appears to be more perpendicular to the membrane surface than that with (160°, 60°) orientation.