Direct observation of binding between biotinylated okadaic acids and protein phosphatase 2A monitored by surface plasmon resonance

Keiichi Konoki, Naoyuki Sugiyama, Michio Murata, Kazuo Tachibana

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

Two biotin conjugates of okadaic acid were synthesized for evaluating their interactions with protein phosphatase 2A by surface plasmon resonance (SPR). C7-biotinylated okadaic acid revealed strong binding affinity to the enzyme, while C1-biotinylated derivative being devoid of affinity, implying that the C7-biotin conjugate is a useful tool for biochemical studies of protein phosphatase 2A.

Original languageEnglish
Pages (from-to)887-890
Number of pages4
JournalTetrahedron Letters
Volume40
Issue number5
DOIs
Publication statusPublished - 1999 Jan 29

Keywords

  • Okadaic acid
  • Protein phosphatases
  • Surface plasmon resonance

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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