論文

査読有り
2018年4月1日

Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism

Biophysical Reviews
  • Yuji Goto
  • ,
  • Masayuki Adachi
  • ,
  • Hiroya Muta
  • ,
  • Masatomo So

10
2
開始ページ
493
終了ページ
502
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1007/s12551-017-0370-7
出版者・発行元
Springer Verlag

Amyloid fibrils are misfolded forms of proteins and are involved in various diseases. They have been studied extensively with the aim to obtain a comprehensive understanding of protein folding and misfolding and to use this knowledge to develop therapeutic strategies against the associated diseases. Salt conditions are important factors determining the formation and stability of amyloid fibrils. In the 1990s, salt effects were studied extensively to understand the conformational stability of acid-denatured proteins, and the results of these studies revealed the role of electrostatic repulsion in forming the compact intermediate states. In this review, we compare the effects of salts on the compact intermediate states with those on the formation of amyloid fibrils under acidic conditions. The results argue that both protein folding and misfolding are driven by the same forces, although the resultant conformations are distinct because they are monomeric and multimeric reactions, respectively.

リンク情報
DOI
https://doi.org/10.1007/s12551-017-0370-7
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/29256120

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