Selection of peptide inhibitors of soluble Aβ1-42 oligomer formation by phage display
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- KAWASAKI Takayasu
- The University of Tokyo, Institute of Industrial Science
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- ONODERA Kenji
- The University of Tokyo, Institute of Industrial Science
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- KAMIJO Shunsuke
- The University of Tokyo, Institute of Industrial Science
書誌事項
- タイトル別名
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- Selection of Peptide Inhibitors of Soluble A.BETA.1-42 Oligomer Formation by Phage Display
- Selection of peptide inhibitors of soluble A v 1 42 oligomer formation by phage display
- Selection of Peptide Inhibitors of Soluble Aβ<sub>1-42</sub>Oligomer Formation by Phage Display
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抄録
There have been many reports suggesting that soluble oligomers of amyloid β (Aβ) are neurotoxins causing Alzheimer’s disease (AD). Although inhibition of the soluble oligomerization of Aβ is considered to be effective in the treatment of AD, almost all peptide inhibitors have been designed from the β-sheet structure (H14-D23) of Aβ1-42. To obtain more potent peptides than the known inhibitors of the soluble-oligomer formation of Aβ1-42, we performed random screening by phage display. After fifth-round panning of a hepta-peptide library against soluble Aβ1-42, novel peptides containing arginine residues were enriched. These peptides were found to suppress specifically 37/48 kDa oligomer formation and to keep the monomeric form of Aβ1-42 even after 24 h of incubation, as disclosed by SDS–PAGE and size-exclusion chromatography. Thus we succeeded in acquiring novel efficient peptides for inhibition of soluble 37/48 kDa oligomer formation of Aβ1-42.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 74 (11), 2214-2219, 2010
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206479425664
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- NII論文ID
- 10027561334
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 10899503
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用不可