Hermetter A, Lakowicz J R
J Biol Chem. 1986 Jun 25;261(18):8243-8.
We used fluorescence non-radiative energy transfer to measure the self-association of melittin in solution and when bound to lipid bilayers. Energy transfer occurred from the tryptophan residue of unlabeled melittin to an N-methyl anthraniloyl residue covalently bound to a basic lysine residue on melittin. The extent of energy transfer from tryptophan to the label was found to increase severalfold upon the salt-induced tetramerization of melittin. When bound to vesicles of dimyristoyl-L-alpha-phosphatidylcholine, the extent of energy transfer was found to be equivalent to that of monomeric melittin, irrespective of the presence of monomeric or tetrameric melittin in the aqueous phase. We conclude that membrane-bound melittin is monomeric.
我们利用荧光非辐射能量转移来测量蜂毒肽在溶液中以及与脂质双层结合时的自缔合情况。能量从未标记的蜂毒肽的色氨酸残基转移至与蜂毒肽上一个碱性赖氨酸残基共价结合的N-甲基邻氨基苯甲酰残基。发现随着盐诱导的蜂毒肽四聚化，从色氨酸到标记物的能量转移程度增加了几倍。当与二肉豆蔻酰-L-α-磷脂酰胆碱囊泡结合时，发现能量转移程度与单体蜂毒肽的相当，而与水相中单体或四聚体蜂毒肽的存在无关。我们得出结论，膜结合的蜂毒肽是单体形式的。
