Chiral adaptive recognition with sequence specificity of aromatic dipeptides in aqueous solution by an achiral cage.

ABSTRACT: Sequence-specific recognition of peptides and proteins by synthetic compounds or systems remains a huge challenge in biocompatible media. Here, we report the chiral adaptive recognition (CAR) with sequence specificity of aromatic dipeptides in a purely aqueous solution using an achiral tetraphenylethene-based octacationic cage (1) as both a molecular receptor and chiroptical sensor. 1 can selectively bind and dimerize aromatic dipeptides to form 1 : 2 host-guest complexes with high binding affinity (>10¹⁰ M^-2), especially up to ∼10¹⁴ M^-2 for TrpTrp. Given the dynamic rotational conformation of TPE units, achiral 1 can exhibit chiral adaptive responses with mirror-symmetrical circular dichroism (CD) and circularly polarized luminescence (CPL) spec

SUBMITTER: Cheng L 

PROVIDER: S-EPMC9890615 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature