Recent Applications of High Pressure to the Studies of Amyloid Fibrils

• CHATANI Eri

  Institute for Protein Research, Osaka University

• GOTO Yuji

  Institute for Protein Research, Osaka University

Bibliographic Information

Other Title

• 高圧力をもちいたアミロイド線維研究の展開
• コウアツリョク オ モチイタ アミロイド センイ ケンキュウ ノ テンカイ

Abstract

Pressure is an important perturbant applied in studies of folding and unfolding of globular proteins. Recently, the application of this perturbant has been extended to the study of amyloid fibrils, which will be reviewed here. The effects of pressure on amyloid fibrils seem various, being positive or negative, dependent on the protein species and experimental conditions. Several reports have shown that pressure drives the formation of amyloid fibrils via pressure-induced unfolded structure of proteins. In contrast, there are also several studies showing the pressure-induced depolymerization of amyloid fibrils, suggesting the deficient packing and/or hydration in the fibril structure. Furthermore, a novel adaptation or maturation phenomenon has been found under pressurized conditions, demonstrating the structural diversity of amyloid fibrils, one of unique features which cannot be predicted with Anfinsen's dogma.

Journal

• The Review of High Pressure Science and Technology

  The Review of High Pressure Science and Technology 17 (1), 42-49, 2007

  The Japan Society of High Pressure Science and Technology

Keywords

• amyloid fibril
• aggregation
• protein folding and misfolding
• packing
• hydration
• adaptation
• maturation

Details

• CRID: 1390282679358845952
• NII Article ID: 10018918410
• NII Book ID: AN10452913
• DOI: 10.4131/jshpreview.17.42
• ISSN: 13481940
• ISSN: 0917639X
• NDL BIB ID: 8742686
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I8742686
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed