Systematic chemical synthesis and structure-function analysis of glycosylated collagens

2016 Fiscal Year Final Research Report

• Project/Area Number: 15K16556
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Biomolecular chemistry
• Research Institution: Tokyo University of Science
• Principal Investigator: HACHISU Masakazu 東京理科大学, 基礎工学部生物工学科, 助教 (60587442)
• Project Period (FY): 2015-04-01 – 2017-03-31
• Keywords: 翻訳後修飾 / ヒドロキシリシン / グリコシル化 / コラーゲン / ペプチド固相合成

Outline of Final Research Achievements

Collagen is the most abundant fibrous protein in animals, constituting dermis, bone and cartilage. The lysine residues in collagen peptide chain are oxidized to collagen-specific hydroxylysine residues by post-translational modification (PTM). Further PTMs of hydrosylysine residues generate the unique glyco-amino acid residues, 2-O-α-D-glucopyranosyl-O-β-D-galactopyranosyl hydroxylysine. The detailed biological functions of the modified lysine residue have not been clearly understood. The purpose of this study is to prepare the glycosylated collagen models. The novel Fmoc-protected glyco-amino acids toward the solid-phase peptide synthesis were designed.

Free Research Field

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