P28 超音波強度に依存したアミロイド線維とアモルファス凝集の形成

DOI

書誌事項

タイトル別名
  • P28 Ultrasonic power-dependent competitive formation of amyloid fibrils and amorphous aggregates

抄録

Amyloid fibrils and amorphous aggregates are two types of aberrant protein aggregates. Amyloid fibrils have highly ordered structure called cross-β structure. On the other hand, amorphous aggregates have no ordered structure. It is known that these two types of aggregates are associated with many serious diseases (e.g. Alzheimer’s and Parkinson’s diseases, dialysis-related amyloidosis). Moreover, protein aggregates are important in industries. For an example, antibodies stored at high concentrations have been known to aggregate, reducing the quality of antibody drugs. Furthermore, the spider silk has ordered β-structure like amyloid fibrils, representing a type of functional amyloids. Thus, the study of the formation of protein aggregates will contribute not only to preventing various diseases and developing therapeutic strategies but also to creating functional amyloids. The aim of this work is to understand the comprehensive mechanism of amyloid fibrillation and amorphous aggregation. With β2-microglobulin (β2m) and ultrasonic irradiation, we investigated the competition between amyloid fibrillation and amorphous aggregation. The results confirmed that ultrasonic irradiation is an effective method for accelerating amyloid fibrillation. We show that the rate of amyloid fibrillation depends on the ultrasonic energy. Moreover, we found that fibril-like aggregates was generated by ultrasonic irradiation. Consequently, we propose a competitive mechanism of amyloid fibrillation, amorphous aggregation and fibril-like aggregation useful for comprehensive understanding of protein aggregation.

収録刊行物

キーワード

詳細情報 詳細情報について

  • CRID
    1390001206052803072
  • NII論文ID
    130005830690
  • DOI
    10.20577/pamjss.25.0_87
  • 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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