Cation-pi interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
Cation-pi interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
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DOI：
10.1126/science.271.5246.163
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发表时间：
1996-01-12
期刊：
影响因子：
56.9
通讯作者：
Dougherty, DA
中科院分区：
文献类型：
--
作者：
Dougherty, DA
阳离子通过一种非常强的非共价力（称为阳离子-π相互作用）结合到芳香结构的表面。该效应的大小和普遍性已通过气相测量和水介质中模型受体的研究确定。对于一级，相互作用可以被认为是正电荷和芳族化合物的四极矩之间的静电吸引力。大量直接和间接证据表明，阳离子-π 相互作用对于结合阳离子配体或底物的多种蛋白质非常重要。在这种情况下，氨基酸苯丙氨酸 (Phe)、酪氨酸 (Tyr) 和色氨酸 (Trp) 可被视为极性但疏水的残基。
Cations bind to the ir face of an aromatic structure through a surprisingly strong, noncovalent force termed the cation-pi interaction. The magnitude and generality of the effect have been established by gas-phase measurements and by studies of model receptors in aqueous media. To first order, the interaction can be considered an electrostatic attraction between a positive charge and the quadrupole moment of the aromatic. A great deal of direct and circumstantial evidence indicates that cation-pi interactions are important in a variety of proteins that bind cationic ligands or substrates. In this context, the amino acids phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp) can be viewed as polar, yet hydrophobic, residues.