Controlled production of amyloid beta peptide from a photo-triggered, water-soluble precursor "click peptide"

Taniguchi, Atsuhiko, Skwarczynski, Mariusz, Sohma, Youhei, Okada, Takuma, Ikeda, Keisuke, Prakash, Halan, Mukai, Hidehito, Hayashi, Yoshio, Kimura, Tooru, Hirota, Shun, Matsuzaki, Katsumi and Kiso, Yoshiaki (2008) Controlled production of amyloid beta peptide from a photo-triggered, water-soluble precursor "click peptide". ChemBioChem, 9 18: 3055-3065. doi:10.1002/cbic.200800503


Author Taniguchi, Atsuhiko
Skwarczynski, Mariusz
Sohma, Youhei
Okada, Takuma
Ikeda, Keisuke
Prakash, Halan
Mukai, Hidehito
Hayashi, Yoshio
Kimura, Tooru
Hirota, Shun
Matsuzaki, Katsumi
Kiso, Yoshiaki
Title Controlled production of amyloid beta peptide from a photo-triggered, water-soluble precursor "click peptide"
Journal name ChemBioChem   Check publisher's open access policy
ISSN 1439-7633
1439-4227
Publication date 2008-12-15
Year available 2008
Sub-type Article (original research)
DOI 10.1002/cbic.200800503
Volume 9
Issue 18
Start page 3055
End page 3065
Total pages 11
Place of publication Weinheim, Germany
Publisher Wiley - VCH Verlag
Language eng
Formatted abstract
In biological experiments, poor solubility and uncontrolled assembly of amyloid beta peptide (Abeta) 1-42 pose significant obstacles to establish an experiment system that clarifies the function of Abeta1-42 in Alzheimer's disease (AD). Herein, as an experimental tool to overcome these problems, we developed a water-soluble photo-"click peptide" with a coumarin-derived photocleavable protective group that is based on an O-acyl isopeptide method. The click peptide had nearly 100-fold higher water solubility than Abeta1-42 and did not self-assemble, as the isomerized structure in its peptide backbone drastically changed the conformation that was derived from Abeta1-42. Moreover, the click peptide afforded Abeta1-42 quickly under physiological conditions (pH 7.4, 37 degrees C) by photoirradiation followed by an O-N intramolecular acyl migration. Because the in situ production of intact Abeta1-42 from the click peptide could improve the difficulties in handling Abeta1-42 caused by its poor solubility and highly aggregative nature, this click peptide strategy would provide a reliable experiment system for investigating the pathological function of Abeta1-42 in AD.
Keyword Biochemistry & Molecular Biology
Chemistry, Medicinal
Biochemistry & Molecular Biology
Pharmacology & Pharmacy
BIOCHEMISTRY & MOLECULAR BIOLOGY
CHEMISTRY, MEDICINAL
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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Created: Mon, 21 Mar 2011, 09:01:03 EST by Dr Mariusz Skwarczynski on behalf of School of Chemistry & Molecular Biosciences