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• W2092551667 abstract "Melittin possesses an amphiphilic property in the primary sequence in which hydrophilic residues are located at the C-terminal region from Lys-21 to Gln-26. A part of the hydrophilic sequence was cleaved off by endopeptidase ArgC to obtain melittin 1–22. The affinity of melittin 1–22 for neutral phospholipid membrane was reduced to 13 that of melittin, indicating that the basic residues, Lys-23 and Arg-24, are important in binding of melittin to the membrane. The melittin 1–22 was extended toward the C-terminal end by connection of lactose (melittin-lac), the membrane affinity of which was slightly higher than the melittin 1–22, but lower than melittin. The leakage experiment of 5,6-carboxyfluorescein encapsulated in DPPC liposomes showed that the activities of melittin 1–22 and melittin-lac in membrane lysis were much lower than melittin. However, the melittin 1–22 formed a voltage-dependent ion-channel in an azolectin bilayer membrane. It is thus considered that Lys-23 and Arg-24 residues of melittin play an important role in binding to the polar region of membrane for lysis, but not for ion-channel formation." @default.
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• W2092551667 date "1992-11-01" @default.
• W2092551667 modified "2023-10-17" @default.
• W2092551667 title "Interaction of melittin derivatives with lipid bilayer membrane. Role of basic residues at the C-terminal and their replacement with lactose" @default.
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• W2092551667 doi "https://doi.org/10.1016/0005-2736(92)90245-h" @default.
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