title: Dual native chemical ligation at lysine.
abstract: A thiol group introduced on the gamma-carbon of lysine mediates robust native chemical ligation at both the alpha- and epsilon-amines in two consecutive steps. Desulfurization then affords the final product, in which the lysine residue at the ligation site has an isopeptide bond on its side chain. The method is useful for the synthesis of proteins containing special post-translational modifications on lysine.
authors.affiliation: Division of Chemical Biology and Biotechnology, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
authors.forename: Renliang
authors.initials: R
authors.lastname: Yang
authors.forename: Kalyan Kumar
authors.initials: KK
authors.lastname: Pasunooti
authors.forename: Fupeng
authors.initials: F
authors.lastname: Li
authors.forename: Xue-Wei
authors.initials: XW
authors.lastname: Liu
authors.forename: Chuan-Fa
authors.initials: CF
authors.lastname: Liu
mesh_terms: D000588:Amines / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry* / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000138:chemical synthesis* / Q000378:metabolism
chemical_list: D000588:Amines; D011506:Proteins; D008239:Lysine