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456 investigated how the YEATS domain of human reader protein AF9 recognizes both Kac and Kcr by incorporating para -substituted phenylalanine derivatives (R = CH 3 , Cl, CN, or NO 2 ) with distinct electrostatic properties at two specific positions (Phe28 and Tyr78) via GCE and revealed that the amide−π interactions between AF9 and acyllysines can be fine-tuned by altering the electron-rich nature of the aromatic rings, with more electron-rich rings resulting in more favorable interactions, which contrasts with amide–heteroarene interactions and offers valuable insights for potential therapeutic applications

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