Chemo-enzymatic synthesis of a bioactive peptide containing a glutamine-linked oligosaccharide and its characterization |
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| Affiliation: | 1. The Noguchi Institute, 1-8-1 Kaga, Itabashi, Tokyo 173-0003, Japan;2. Graduate School of Biostudies, Kyoto University, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan;3. Institute for Applied Biochemistry, University of Tsukuba, Tennodai, Tsukuba 305, Japan;3. Institutes of Biomedicine, University of Eastern Finland, P. O. Box 1627, FIN-70210 Kuopio, Finland;4. Institutes of Dentistry, School of Medicine, University of Eastern Finland, P. O. Box 1627, FIN-70210 Kuopio, Finland;1. Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, the Netherlands |
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| Abstract: | A bioactive peptide containing a glutamine-linked oligosaccharide was chemo-enzymatically synthesized by use of the solid-phase method of peptide synthesis and the transglycosylation activity of endo-β-N-acetylglucosaminidase. Substance P, a neuropeptide, is an undecapeptide containing two l-glutamine residues. A substance P derivative with an N-acetyl-d-glucosamine residue attached to the fifth or sixth l-glutamine residue from the N-terminal region was chemically synthesized. A sialo complex-type oligosaccharide derived from a glycopeptide of hen egg yolk was added to the N-acetyl-d-glucosamine moiety of the substance P derivative using the transglycosylation activity of endo-β-N-acetylglucosaminidase from Mucor hiemalis, and a substance P derivative with a sialo complex-type oligosaccharide attached to the l-glutamine residue was synthesized. This glycosylated substance P was biologically active, although the activity was rather low, and stable against peptidase digestion. The oligosaccharide moiety attached to the l-glutamine residue of the peptide was not liberated by peptide-N4-(N-acetyl-β-d-glucosaminyl) asparagine amidase F. |
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