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.
|Number of pages||7|
|Journal||International Journal of Peptide Research and Therapeutics|
|Publication status||Published - 2007 Jun|
- Horner-Emmons reaction
- Solid-phase synthesis
- Substrate specificity