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Published on: July 11, 2020
Total synthesis of biotinylated N domain of human hepatocyte growth factor
Laurent Raibaut1, Jérome Vicogne, Bérénice Leclercq
1UMR CNRS 8161 Univ Lille Nord de France, Institut Pasteur de Lille, 1 rue du Pr Calmette, Lille 59021, France.
Abstract:
Hepatocyte growth factor/scatter factor (HGF/SF) is the high affinity ligand of MET tyrosine kinase receptor. We report here the total synthesis of a biotinylated analogue of human HGF/SF N domain. Functionally, N domain is part of the HGF/SF high affinity binding site for MET and also the main HGF/SF binding site for heparin. The 97 Aa linear chain featuring a C-terminal biotin group was assembled in high yield using an N-to-C one-pot three segments assembly strategy relying on a sequential Native Chemical Ligation (NCL)/bis(2-sulfanylethyl)amido (SEA) native peptide ligation process. The folded protein displayed the native disulfide bond pattern and showed the ability to bind heparin.

