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Journal Articles Journal of Molecular Biology Year : 2000

Stabilization of bound polycyclic aromatic hydrocarbons by a π-cation interaction

Abstract

Proteins can use aromatic side-chains to stabilize bound cationic ligands through cation-p interactions. Here, we report the ®rst example of the reciprocal process, termed p-cation, in which a cationic protein side-chain stabilizes a neutral aromatic ligand. Site-directed mutagenesis revealed that an arginine side-chain located in the deep binding pocket of a monoclonal antibody (4D5) is essential for binding the neutral polynuclear aromatic hydrocarbon benzo[a]pyrene. This Arg was very likely selected for in the primary response, further underscoring the importance of the p-cation interaction for ligand binding, which should be considered in protein analysis and design when ligands include aromatic groups.

Dates and versions

hal-03274031 , version 1 (29-06-2021)

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Jean-Luc Pellequer, Bitao Zhao, Hui-I. Kao, Christopher W Bell, Kai Li, et al.. Stabilization of bound polycyclic aromatic hydrocarbons by a π-cation interaction. Journal of Molecular Biology, 2000, 302 (3), pp.691-699. ⟨10.1006/jmbi.2000.4033⟩. ⟨hal-03274031⟩
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