Methionine is the second-rarest amino acid in vertebrates and has been recognized to play a critical role in cellular signaling pathways due to its propensity for oxidation and metal binding. While the other sulfur-containing proteinogenic amino acid, cysteine, has been widely employed for selective bioconjugation methods, methionine bioconjugation remains largely underdeveloped. To meet this challenge, our laboratories developed oxaziridine reagents for selective <i>N</i>-transfer to methionine, which give access to sulfimide conjugates. The utility of this strategy coined ReACT (Redox Activated Chemical Tagging) has been demonstrated in various examples, such as the synthesis of antibody-drug conjugates.<br/>In order to expand the applicability of this bioconjugation method, we have set out to devise reagents which will enable the use of methionine tagging in combination with a variety of well-established labeling reactions. This poster will elaborate on our ongoing efforts to develop heterobifunctional crosslinking reagents incorporating our methionine-reactive oxaziridines. Such an approach is especially interesting in view of the above-mentioned scarcity of methionine, which offers a handle for highly site-selective protein modifications.<br/>

Methionine bioconjugation: Development of heterobifunctional crosslinking reagents

ACS Fall 2020 Virtual Meeting

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