The discovery of peptide assembly strategies that allow expedited and simple access to medium sized proteins of less than 150 amino acids is a challenging goal. Up to now, protein sequential assembly has been mainly carried out using sequential C-to-N Native Chemical Ligations (NCLs). Here we combined NCL chemistry and the unique chemical properties of bis(2-sulfanylethyl)amido (SEA) group in order to design a highly efficient one-pot three segment protein assembly procedure, working in N-to-C direction. The assembly method is compatible with Fmoc solid phase peptide synthesis and is illustrated with the synthesis of biologically active K1 domain from Hepatocyte Growth Factor/Scatter Factor (HGF/SF). Figure 1. <img src='https://acs-archive-assets2.s3.amazonaws.com/239nm/uploads/22521_figure_1.jpg' alt='' /> SEA chemistry: Ollivier, N. Org Lett. 2010 , 12, 5238-41; Dheur, J. Org. Lett. 2011 , 13, 1560-3; Dheur, J. J. Org. Chem. 2011 , 76, 3194-202. Ollivier, N. Angewandte Chemie Int. Ed. 2011 , in press.

Novel strategies for protein total synthesis based on bis(2-sulfanylethyl)amido native peptide ligation

243rd National Meeting (2012)

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