Issue 15, 2003
From the journal:

Organic & Biomolecular Chemistry

Effects of β-sheet breaker peptidepolymers on scrapie-infected mouse neuroblastoma cells and their affinities to prion protein fragment PrP(81–145)

Takehisa Oishi,a   Ken-ichi Hagiwara,b   Tomoya Kinumi,†b   Yoshio Yamakawa,b   Masahiro Nishijima,b   Kazuhiko Nakamurac  and  Hirokazu Arimoto*ad  

* Corresponding authors

a Department of Chemistry, Graduate School of Science, Nagoya University, Chikusa, Nagoya 464-8602, Japan
E-mail: arimoto@org.chem.nagoya-u.ac.jp
Fax: +81-52-789-5041

b Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan

c Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8566, Japan

d Institute for Advanced Research, Nagoya University; and PRESTO, JST, Chikusa, Nagoya 464-8602, Japan

Abstract

The effects of Soto's ‘β-sheet breaker peptide’ and its polymer on PrPSc formation in ScN2a cells were investigated. Surface plasmon resonance study indicated that direct binding between PrP(81–145) and the ‘β-sheet breaker peptide’ is not specific and may not play a major role in the inhibition of PrPSc formation.

Graphical abstract: Effects of β-sheet breaker peptide polymers on scrapie-infected mouse neuroblastoma cells and their affinities to prion protein fragment PrP(81–145)

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Article information

DOI
https://doi.org/10.1039/B306682G
Article type
Communication
Submitted
16 Jun 2003
Accepted
03 Jul 2003
First published
09 Jul 2003

Org. Biomol. Chem., 2003,1, 2626-2629

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Effects of β-sheet breaker peptide polymers on scrapie-infected mouse neuroblastoma cells and their affinities to prion protein fragment PrP(81–145)

T. Oishi, K. Hagiwara, T. Kinumi, Y. Yamakawa, M. Nishijima, K. Nakamura and H. Arimoto, Org. Biomol. Chem., 2003, 1, 2626 DOI: 10.1039/B306682G

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