HPLC and MS Studies of Orientation of Melittin on Phospholipid Membrane.
The orientation of melittin binding to liposomes with or without transmembrane potential was investigated. With a combination of high performance liquid chromatography and mass spectrometry, the membrane association state of melittin was detected by analyzing its trypsin-digested products. It was found that the enzyme could access all the proteolytic sites on protein binding to the liposome without membrane potential, while one proteolytic site on the N-terminal of the protein was blocked after it binding to the liposome with negative transmembrane potential. The results showed that melittin changed its orientation in the latter case.
Beijing Institute of Microchemistry, Beijing 100091, China. wuyi@ns.ciii.com.cn
Wei
W
Niu
Yi
Y
Wu
Yu-Feng
YF
Yang
Sen-Fang
SF
Sui