Journal
NATURE PROTOCOLS
Volume 10, Issue 2, Pages 269-292Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nprot.2015.013
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Funding
- Centre National de la Recherche Scientifique (CNRS)
- University of Lille
- Institut Pasteur de Lille
- Site de Recherche Integree sur le Cancer (SIRIC) OncoLille
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Small ubiquitin-like modifier (SUMO) post-translational modification (PTM) of proteins has a crucial role in the regulation of important cellular processes. This protocol describes the chemical synthesis of functional SUMO-peptide conjugates. The two crucial stages of this protocol are the solid-phase synthesis of peptide segments derivatized by thioester or bis(2-sulfanylethyl) amido (SEA) latent thioester functionalities and the one-pot assembly of the SUMO-peptide conjugate by a sequential native chemical ligation (NCL)/SEA native peptide ligation reaction sequence. This protocol also enables the isolation of a SUMO SEA latent thioester, which can be attached to a target peptide or protein in a subsequent step. It is compatible with 9-fluorenylmethoxycarbonyl (Fmoc) chemistry, and it gives access to homogeneous, reversible and functional SUMO conjugates that are not easily produced using living systems. The synthesis of SUMO-peptide conjugates on a milligram scale takes 20 working days.
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