Evaluation of superior BACE1 cleavage sequences containing unnatural amino acids

Taeko Kakizawa, Akira Sanjoh, Akane Kobayashi, Yasunao Hattori, Kenta Teruya, Kenichi Akaji

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

A recombinant form of BACE1 (β-site amyloid precursor protein cleaving enzyme-1) corresponding to positions 46-454 of the extracellular domain of the original membrane enzyme was prepared. The recombinant BACE1 (rBACE1) had the kinetic parameters Km = 5.5 μM and kcat = 1719 s -1. Using several libraries of substrates containing unnatural amino acids, the specificity of rBACE1 was evaluated. LC/MS of digests derived from the libraries clarified that a dodecapeptide containing unnatural amino acids at P2 to P1 was a superior cleavage sequence.

Original languageEnglish
Pages (from-to)2785-2789
Number of pages5
JournalBioorganic and Medicinal Chemistry
Volume19
Issue number9
DOIs
Publication statusPublished - 2011 May 1
Externally publishedYes

Keywords

  • Amyloid peptide
  • BACE1
  • Substrate specificity
  • Unnatural amino acid

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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