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Hydrophilic ligand enables efficient bioconjugation of proteins with post-translational modifications in water, suggesting advances in peptide chemistry.
The selective and natural post-translational modification of peptides and proteins under biocompatible conditions remains a challenge. Herein, we report a hydrophilic variant of the BIPHEPHOS ligand featuring diethyl phosphonates as solubilizing groups, which were found to be catalytically isofunctional to unpolar tert-butyl. This enabled the fast introduction of native prenyl groups and bioconjugation handles into peptides and folded proteins under nearly aqueous conditions.
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Schlatzer et al. (2025) studied this question.
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