Experimental Study on the Mechanism Underlying the Anti-aggregation Function of a Group3LEA Peptide

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  • YAMAKAWA Kentaro
    Center for Biological Resources and Informatics, Tokyo Institute of Technology
  • FURUKI Takao
    Center for Biological Resources and Informatics, Tokyo Institute of Technology
  • FURUTA Tadaomi
    Center for Biological Resources and Informatics, Tokyo Institute of Technology
  • HATANAKA Rie
    National Institute of Agrobiological Sciences(NIAS)
  • KIKAWADA Takahiro
    National Institute of Agrobiological Sciences(NIAS)
  • NIWA Tatsuya
    Department of Biomolecular Engineering, Tokyo Institute of Technology
  • TAGUCHI Hideki
    Department of Biomolecular Engineering, Tokyo Institute of Technology
  • FURUSAWA Hiroyuki
    Department of Biomolecular Engineering, Tokyo Institute of Technology
  • OKAHATA Yoshio
    Department of Biomolecular Engineering, Tokyo Institute of Technology
  • SAKURAI Minoru
    Center for Biological Resources and Informatics, Tokyo Institute of Technology

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Other Title
  • Group3LEAペプチドのタンパク質凝集抑制メカニズムに関する実験的研究
  • Group3LEA ペプチド ノ タンパクシツ ギョウシュウ ヨクセイ メカニズム ニ カンスル ジッケンテキ ケンキュウ

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Abstract

We show that a short model peptide which has two tandem repeats of the 11-mer motif of a group3 late embryogenesis abundant protein protects proteins against aggregation by desiccation stress. Next, we measure the dissociation constant between the LEA model peptide and its partner protein (lysozyme and HybD) using quartz crystal microbalance (QCM) method. Similar experiments are performed for a native LEA protein from the anhydrobiotic nematode A. avenae. On the basis of these results, the mechanism of the anti-aggregation function of the LEA peptide is discussed.

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