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 language | English |
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Pages (from-to) | 173-179 |
Number of pages | 7 |
Journal | International Journal of Peptide Research and Therapeutics |
Volume | 13 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 2007 Jun |
Externally published | Yes |
Keywords
- HTLV-1
- Horner-Emmons reaction
- Solid-phase synthesis
- Substrate specificity
ASJC Scopus subject areas
- Analytical Chemistry
- Bioengineering
- Biochemistry
- Molecular Medicine
- Drug Discovery