Design of Artificial Proteins and Peptides Targeting to Amyloid .BETA. Peptide (A.BETA.) and Control of A.BETA. Aggregation
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- TAKAHASHI Tsuyoshi
- Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
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- MATSUMURA Sachiko
- JST / Department of Protein Engineering, The Cancer Institute, Japanese Foundation for Cancer Research
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- MIHARA Hisakazu
- Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
Bibliographic Information
- Other Title
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- アミロイドβペプチド(Aβ)を標的とした人工タンパク質・ペプチドの設計とAβ集合体形成の制御
- アミロイドβペプチド(Aβ)を標的とした人工タンパク質・ベプチドの設計とAβ集合体形成の制御
- アミロイド ベータ ペプチド A ベータ オ ヒョウテキ ト シタ ジンコウ タンパクシツ ベプチド ノ セッケイ ト A ベータ シュウゴウタイ ケイセイ ノ セイギョ
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Abstract
Misfolding of proteins is of relevance to a variety of fatal diseases, which include Alzheimer’s disease (AD) and prion disease. In the case of AD, amyloid fibril composed of the amyloid β peptide (Aβ) is a principal component of the cerebral plaques found in the brains of patients. Monomeric Aβ is assembled into amyloid fibrils via oligomeric state. To construct the molecules that bind to Aβ and control the fibrillogenesis, we have designed the artificial proteins using green fluorescent protein (GFP) with Aβ sequences. The proteins can inhibit the oligomerization of Aβ1-42 by binding strongly to Aβ molecule. We have also designed the peptides capable of forming amyloid-like fibrils by amplifying and capturing Aβ amyloid fibrils and soluble Aβ oligomers. These studies might contribute to understanding how protein misfolds and what happens during the protein misfolding.<br>
Journal
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- Seibutsu Butsuri
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Seibutsu Butsuri 47 (4), 228-234, 2007
The Biophysical Society of Japan General Incorporated Association
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Keywords
Details 詳細情報について
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- CRID
- 1390282681511058432
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- NII Article ID
- 110006369066
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- NII Book ID
- AN00129693
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- ISSN
- 13474219
- 05824052
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- NDL BIB ID
- 8900471
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed