Chemical synthesis of intentionally misfolded homogeneous glycoprotein: a unique approach for the study of glycoprotein quality control |
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Authors: | Izumi Masayuki Makimura Yutaka Dedola Simone Seko Akira Kanamori Akiko Sakono Masafumi Ito Yukishige Kajihara Yasuhiro |
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Affiliation: | Department of Chemistry, Graduate School of Science, Osaka University, Toyonaka, Osaka, 560-0043 Japan. |
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Abstract: | Biosynthesis of glycoproteins in the endoplasmic reticulum employs a quality control system, which discriminates and excludes misfolded malfunctional glycoproteins from a correctly folded one. As chemical tools to study the glycoprotein quality control system, we systematically synthesized misfolded homogeneous glycoproteins bearing a high-mannose type oligosaccharide via oxidative misfolding of a chemically synthesized homogeneous glycopeptide. The endoplasmic reticulum folding sensor enzyme, UDP-glucose:glycoprotein glucosyltransferase (UGGT), recognizes a specific folding intermediate, which exhibits a molten globule-like hydrophobic nature. |
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