New Selenium-Mediated Methods for Protein Synthesis and Modification — ASN Events
  1. Schedule
  2. SESSION 9: CIPPS
  3. New Selenium-Mediated Methods for Protein Synthesis and Modification

New Selenium-Mediated Methods for Protein Synthesis and Modification (#49)

Emma E Watson 1 , Sameer S Kulkarni 2 , Joshua W. C. Maxwell 2 , Jason Johansen-Leete 2 , Luke J Dowman 2 , Andrew M Giltrap 2 , Alexander R Norman 2 , Christian C. F. W. Becker 3 , Richard J Payne 2
  1. The University of Adelaide, Adelaide, SOUTH AUSTRALIA, Australia
  2. School of Chemistry, The University of Sydney, Sydney, NSW, Australia
  3. Institute of Biological Chemistry, University of Vienna, Vienna, Austria

Selenium provides unique opportunities in the chemical synthesis and modification of proteins owing to its enhanced reactivity compared to corresponding sulfur-containing components. We have extended the application of such reactivity to expressed protein fragments through the conversion of C-terminal acyl hydrazides to the corresponding selenoesters which provide valuable intermediates for the synthesis of proteins with modifications near their C-terminus via the Diselenide-Selenoester Ligation (DSL).1 These selenoesters can also be used for the incorporation of diselenides into expressed proteins to serve as substrates for late-stage modification via Photocatalytic Diselenide Contraction (PDC).2 Taken together, these technologies allow us to access pure samples of homogenously modified proteins for downstream evaluation to elucidate the functional roles of natural and designer modifications, alike.

1 S. S. Kulkarni*, E. E. Watson*, J. W. C. Maxwell, G. Niederacher, J. Johansen-Leete, S. Huhmann, S. Mukherjee, A. R. Norman, J. Kriegesmann, C. F. W. Becker, R. J. Payne, Angew. Chem. Int. Ed. 2022, 61, e202200163.

2 L. J. Dowman, S. S. Kulkarni, J. V. Alegre-Requena, A. M. Giltrap, A. R. Norman, A. Sharma, L. C. Gallegos, A. S. Mackay, A. P. Welegedara, E. E. Watson, D. van Raad, G. Niederacher, S. Huhmann, N. Proschogo, K. Patel, M. Larance, C. F. W. Becker, J. P. Mackay, G. Lakhwani, T. Huber, R. S. Paton, R. J. Payne, Nat. Commun. 2022, 13, 6885.

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