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KAKEN_15K01806seika.pdf
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:175.8 KB
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| Last updated |
:Nov 12, 2018 |
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Total downloads since Nov 12, 2018 : 449
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| Title |
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難合成糖鎖受容体を分子模倣した修飾ペプチドの活性機構解明
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ナンゴウセイ トウサ ジュヨウタイ オ ブンシ モホウシタ シュウショク ペプチド ノ カッセイ キコウ カイメイ
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Nangōsei tōsa juyōtai o bunshi mohōshita shūshoku pepuchido no kassei kikō kaimei
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Inhibition mechanism of modified peptide ligands that mimic complicated sugar receptors
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松原, 輝彦
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マツバラ, テルヒコ
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Matsubara, Teruhiko
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慶應義塾大学・理工学部・講師
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Research team head
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科研費研究者番号 : 10325251
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藤原, 由梨奈
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フジワラ, ユリナ
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Fujiwara, Yurina
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Research team member
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2018
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科学研究費補助金研究成果報告書
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2017
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| Abstract |
天然リガンドの代わりに認識される分子を合理設計するため, インフルエンザウイルスのヘマグルチニン(HA)を標的としたペプチドの相互作用解析を行った。糖鎖受容体の代わりに認識されて感染阻害を行う糖修飾ペプチドのHAおよび感染細胞との相互作用解析を行った。糖修飾ペプチドは設計通りHAの糖鎖結合受容体に結合することがわかったが, ペプチド共存下で細胞のエンドサイトーシスを抑制させても感染が抑制されず, HAとの相互作用が感染阻害活性に直接関わっていないことが示唆された。これらの結果は, 糖修飾ペプチドが細胞内での膜融合を阻害している可能性を示し, 新規な阻害機構を有するペプチドリガンドとして期待出来る。
Toward design of artificial peptide ligands by de novo, the interaction between hemagglutinin (HA) and peptides that bind to HA of influenza virus were investigated. Sugar-modified peptide showed the binding to the sugar receptor-binding site, but the peptide could not inhibit endocytosis induced by viral infection. This result suggests that the peptide is not directly inhibited the initial attachment of virus to sugar receptor on cell surface. Several analyses indicate that the sugar-modified peptide has a potential to inhibit membrane fusion after endocytosis. This kind of peptide with inhibition of membrane fusion is an unique activity, suggesting that it is useful for designing of peptide ligands with novel mechanism of inhibition for viral infection.
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研究種目 : 基盤研究(C)(一般)
研究期間 : 2015～2017
課題番号 : 15K01806
研究分野 : 生体分子科学
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