P29 超音波によるニワトリ卵白リゾチームのアミロイド線維形成反応の促進

DOI

書誌事項

タイトル別名
  • P29 Amyloid fibrillation of hen egg white lysozyme accelerated by ultrasonication

抄録

Although proteins generally fold into a specific native structure, aberrant aggregates sometimes form. It is known that there are two types of aggregates, i.e. amyloid fibrils and amorphous aggregates. Amyloid fibrils have ordered cross β structure. On the other hand, amorphous aggregates have no or less ordered structure. These aggregates are associated with various diseases such as Alzheimer’s disease. Recently, the effects of additives on acceleration or inhibition of aggregation have been highlighted. However, the relation between the effects of additive and aggregation mechanisms is still unclear. In this study, we focused on the effects of heparin, used as an anticoagulant agent, on fibrillation of hen egg white lysozyme (HEWL). At first, amyloid fibrils were induced by adding a low concentratios of heparin under acidic conditions where no fibrillation occurred. However, exceeding a certain heparin concentration (1 mg/mL), amorphous aggregation occurred immediately. Interestingly, at a higher heparin concentration (37 mg/ml) under ultrasonication, amorphous aggregation did not occurr but amyloid fibrillation occurred again. These results, we suggest that heparin showed the concentration-dependent acceleration or inhibition of fibrillation. We propose a new viewpoint of the salt-dependent aggregation mechanism of proteins. This suggests that amyloid fibrils and amorphous aggregates form competitively depending on concentrations of additives. The interpretation that amyloid fibrils are in a close relationship with amorphous aggregates. These interpretation will be important to revealing the fibrillation mechanism.

収録刊行物

キーワード

詳細情報 詳細情報について

  • CRID
    1390282681029512320
  • NII論文ID
    130005830689
  • DOI
    10.20577/pamjss.25.0_89
  • ISSN
    24241512
  • 本文言語コード
    ja
  • データソース種別
    • JaLC
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

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