Reversible
Native Chemical Ligation: A Facile Access
to Dynamic Covalent Peptides
Yves Ruff
Valentina Garavini
Nicolas Giuseppone
10.1021/ja4129845.s001
https://acs.figshare.com/articles/journal_contribution/Reversible_Native_Chemical_Ligation_A_Facile_Access_to_Dynamic_Covalent_Peptides/2302132
The
broad interest of using reversible covalent bonds in chemistry,
in particular at its interfaces with biology and materials science,
has been recently established through numerous examples in the literature.
However, the challenging exchange of peptide fragments using a dynamic
covalent
peptide bond has not yet been achieved without enzymatic catalysis
because of its high thermodynamic stability. Here we show that peptide
fragments can be exchanged by a chemoselective and reversible native
chemical ligation (NCL) which can take place at <i>N</i>-(methyl)-cysteine residues. This very mild reaction is efficient
in aqueous solution, is buffered at physiological pH in the presence
of dithiothreitol (DTT), and shows typical half-times of equilibration
in the 10 h range.
2014-04-30 00:00:00
DTT
Reversible Native Chemical Ligation
Dynamic Covalent PeptidesThe
peptide fragments
10 h range
covalent peptide bond
NCL