Calculation of the magnitude and orientation of electrostatic interactions between small aromatic rings in peptides and proteins: Implications for angiotensin II

Abstract

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.