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Evaluations of substrate specificity and inhibition at PR/p3 cleavage site of HTLV-1 protease.
Studies on Substrate Specificity at PR/p3 Cleavage Site of HTLV-1 Protease
  • J. Bang, K. Teruya, K. Akaji
  • Biology, Chemistry
    International Journal of Peptide Research and…
  • 10 January 2007
TLDR
From the digestion of substrate peptides by a chemically synthesized mutant of HTLV-1 protease (C2A HT LV-1 PR), it was found for the first time that the preference for Pro at the P1′ position and for Ile at theP2 position is unique for this enzyme.
Total synthesis of human insulin by regioselective disulfide formation using the silyl chloride-sulfoxide method
Total synthesis of human insulin, a two:chain peptide containing three disulfide bonds, was achieved unambiguously by sequential and selective formation of disulfide bonds in the protein for the
Disulfide Bond Formation Using the Silyl Chloride-Sulfoxide System for the Synthesis of a Cystine Peptide
TLDR
This new disulfide bond forming reaction in trifluoroacetic acid is successfully applied to the syntheses of oxytocin, human brain natriuretic peptide, and somatostatin without any solubility problem.
Synthesis of cystine-peptide by a new disulphide bond-forming reaction using the siiyl chloride–sulphoxide system
Methyltrichlorosilane or tetrachlorosilane in trifluoroacetic acid, in the presence of diphenylsulphoxide, is found to cleave various S-protecting groups of cysteine to form cystine directly by the
Synthesis of porcine brain natriuretic peptide-32 using silver tetrafluoroborate as a new deprotecting reagent of the S-trimethylacetamidomethyl group.
TLDR
Newly isolated porcine brain natriuretic peptide-32 (pBNP-32) was synthesized using AgBF4 and Cys(Tacm) derivatives and had the highest chick rectum relaxant activity among the ANP-BNP families.
Deprotection of the S-trimethylacetamidomethyl (Tacm) group using silver tetrafluoroborate: application to the synthesis of porcine brain natriuretic peptide-32 (pBNP-32).
TLDR
A newly isolated porcine brain natriuretic peptide-32 (pBNP-32) was synthesized by the combined use of the S-Tacm group and AgBF4 deprotection, and the recently developed reagent tetrafluoroboric acid (HBF4) was applied to cleave the peptide from the resin.
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