Fowler P W, Moore G J
Department of Chemistry, University of Exeter, U.K.
Biochem Biophys Res Commun. 1988 Jun 30;153(3):1296-300. doi: 10.1016/s0006-291x(88)81369-x.
Electrostatic interactions between aromatic rings are believed to contribute to the intramolecular structuring and biological function of peptides and proteins. The modes of interaction of benzene with 1) benzene (Phe:Phe), 2) imidazole (Phe:His), and 3) imidazole anion (Phe:His), were calculated using all-electron ab initio wavefunctions. In all cases parallel-plate stackings were found to be purely repulsive, whereas perpendicular-plate geometries were attractive with interaction energies of -0.82 (Phe:Phe), -1.19 (Phe:His) and -3.39 (Phe:His) kcal/mole. These data show that small ring interactions in peptides and proteins will prefer perpendicular-plate geometry. For the proposed His:Phe interaction in angiotensin II, the attraction will be three times greater when the imidazole ring carries a negative charge.
芳香环之间的静电相互作用被认为有助于肽和蛋白质的分子内结构形成及生物学功能。使用全电子从头算波函数计算了苯与1）苯（苯丙氨酸：苯丙氨酸）、2）咪唑（苯丙氨酸：组氨酸）和3）咪唑阴离子（苯丙氨酸：组氨酸）的相互作用模式。在所有情况下，平行板堆积被发现是纯粹排斥的，而垂直板几何结构是有吸引力的，相互作用能分别为-0.82（苯丙氨酸：苯丙氨酸）、-1.19（苯丙氨酸：组氨酸）和-3.39（苯丙氨酸：组氨酸）千卡/摩尔。这些数据表明，肽和蛋白质中的小环相互作用将更倾向于垂直板几何结构。对于血管紧张素II中提出的组氨酸：苯丙氨酸相互作用，当咪唑环带负电荷时，吸引力将大三倍。
