Studies on substrate specificity at PR/p3 cleavage site of HTLV-1 protease

Jeong Kyu Bang, Kenta Teruya, Saburo Aimoto, Hiroyuki Konno, Kazuto Nosaka, Tadashi Tatsumi, Kenichi Akaji

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Substrate specificities for recognition at the PR/p3 site of HTLV-1 protease were clarified using small libraries of substrate peptides. Specificities at P1 and P1′ positions were examined by parallel synthesis/digestion of synthetic peptides covering the PR/p3 site (KGPPVILPIQA). Specificities at P2 to P4 positions were examined by split and mix syntheses of olefin-peptide libraries containing the substrate sequence (PPVILPIQ). The solid-phase Horner-Emmons reaction was successfully applied to syntheses of multi-component substrates for library preparation. From the digestion of substrate peptides by a chemically synthesized mutant of HTLV-1 protease (C2A HTLV-1 PR), it was found for the first time that the preference for Pro at the P1′ position and for Ile at the P2 position is unique for this enzyme.

Original languageEnglish
Pages (from-to)173-179
Number of pages7
JournalInternational Journal of Peptide Research and Therapeutics
Volume13
Issue number1-2
DOIs
Publication statusPublished - 2007 Jun

Keywords

  • HTLV-1
  • Horner-Emmons reaction
  • Solid-phase synthesis
  • Substrate specificity

ASJC Scopus subject areas

  • Analytical Chemistry
  • Bioengineering
  • Biochemistry
  • Molecular Medicine
  • Drug Discovery

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