We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable reagents, they can be activated on-demand for enabling ligation reactions down to peptide concentrations as low as a few hundreds nM at rates approaching 30 M -1 s -1 .
Providing biomolecules
with extended physicochemical, biochemical,
or biological properties is a contemporary challenge motivated by
impactful benefits in life or materials sciences. In this study, we
show that a latent and highly reactive oxalyl thioester precursor
can be efficiently introduced as a pending functionality into a fully
synthetic protein domain following a protection/late-stage deprotection
strategy and can serve as an on-demand reactive handle. The approach
is illustrated with the production of a 10 kDa ubiquitin Lys48 conjugate.
We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable reagents, they can be activated on-demand for enabling ligation reactions down to peptide concentrations as low as a few hundreds nM at rates approaching 30 M-1 s-1.
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