Screening of DNA aptamer which binds to α-synuclein

Kaori Tsukakoshi; Ryuichi Harada; Koji Sode; Kazunori Ikebukuro

doi:10.1007/s10529-010-0200-5

Screening of DNA aptamer which binds to α-synuclein

Kaori Tsukakoshi, Ryuichi Harada, Koji Sode, Kazunori Ikebukuro

Research output: Contribution to journal › Article › peer-review

39 Citations (Scopus)

Abstract

α-Synuclein is a native, unfolded protein that causes several neurodegenerative diseases such as dementia with Lewy bodies and Parkinson's disease. We have now identified the first DNA aptamers against α-synuclein using native PAGE applied to the SELEX method. We call this aptamer "M5-15"; it is the α-synuclein-bound aptamer and was isolated after four cycles of screening. M5-15 is composed of three stem-loop structures that may play an important role in the binding to α-synuclein. Moreover, M5-15 specifically binds to the α-synuclein monomer and oligomer. We expect that this aptamer will become a useful tool in α-synuclein analysis and diagnosis.

Original language	English
Pages (from-to)	643-648
Number of pages	6
Journal	Biotechnology Letters
Volume	32
Issue number	5
DOIs	https://doi.org/10.1007/s10529-010-0200-5
Publication status	Published - 2010
Externally published	Yes

Keywords

Alzheimer's disease
DNA aptamer
Lewy bodies
Parkinson's disease
α-Synuclein

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1007/s10529-010-0200-5

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abstract = "α-Synuclein is a native, unfolded protein that causes several neurodegenerative diseases such as dementia with Lewy bodies and Parkinson's disease. We have now identified the first DNA aptamers against α-synuclein using native PAGE applied to the SELEX method. We call this aptamer {"}M5-15{"}; it is the α-synuclein-bound aptamer and was isolated after four cycles of screening. M5-15 is composed of three stem-loop structures that may play an important role in the binding to α-synuclein. Moreover, M5-15 specifically binds to the α-synuclein monomer and oligomer. We expect that this aptamer will become a useful tool in α-synuclein analysis and diagnosis.",

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T1 - Screening of DNA aptamer which binds to α-synuclein

AU - Tsukakoshi, Kaori

AU - Harada, Ryuichi

AU - Sode, Koji

AU - Ikebukuro, Kazunori

PY - 2010

Y1 - 2010

N2 - α-Synuclein is a native, unfolded protein that causes several neurodegenerative diseases such as dementia with Lewy bodies and Parkinson's disease. We have now identified the first DNA aptamers against α-synuclein using native PAGE applied to the SELEX method. We call this aptamer "M5-15"; it is the α-synuclein-bound aptamer and was isolated after four cycles of screening. M5-15 is composed of three stem-loop structures that may play an important role in the binding to α-synuclein. Moreover, M5-15 specifically binds to the α-synuclein monomer and oligomer. We expect that this aptamer will become a useful tool in α-synuclein analysis and diagnosis.

AB - α-Synuclein is a native, unfolded protein that causes several neurodegenerative diseases such as dementia with Lewy bodies and Parkinson's disease. We have now identified the first DNA aptamers against α-synuclein using native PAGE applied to the SELEX method. We call this aptamer "M5-15"; it is the α-synuclein-bound aptamer and was isolated after four cycles of screening. M5-15 is composed of three stem-loop structures that may play an important role in the binding to α-synuclein. Moreover, M5-15 specifically binds to the α-synuclein monomer and oligomer. We expect that this aptamer will become a useful tool in α-synuclein analysis and diagnosis.

KW - Alzheimer's disease

KW - DNA aptamer

KW - Lewy bodies

KW - Parkinson's disease

KW - α-Synuclein

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Screening of DNA aptamer which binds to α-synuclein

Abstract

Keywords

ASJC Scopus subject areas

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