Proline-based tripodal cages with guest-adaptive features for capturing hydrophilic and amphiphilic fluoride substances.

ABSTRACT: Proteins exhibit remarkable molecular recognition by dynamically adjusting their conformations to selectively interact with ligands at specialized binding sites. To bind hydrated ligands, proteins leverage amino acid residues with similar water affinities as the substrate, minimizing the energy required to strip water molecules from the hydrophilic substrates. In synthetic receptor design, replicating this sophisticated adaptability remains a challenge, as most artificial receptors are optimized to bind desolvated substances. Here, we show that proline-based synthetic receptors can mimic the conformational dynamics of proteins to achieve selective binding of hydrophilic and amphiphilic fluoride substances in aqueous environments. This finding highlights the critical role of receptor flexib

SUBMITTER: Huang B 

PROVIDER: S-EPMC11971368 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature