Stolze, Sara C. published the artcileAhp Cyclodepsipeptides: The Impact of the Ahp Residue on the “Canonical Inhibition” of S1 Serine Proteases, Formula: C25H23NO4, the publication is ChemBioChem (2013), 14(11), 1301-1308, database is CAplus and MEDLINE.
S1 serine proteases are by far the largest and most diverse family of proteases encoded in the human genome. Although recent decades have seen an enormous increase in our knowledge, the biol. functions of most of these proteases remain to be elucidated. Chem. inhibitors have proven to be versatile tools for studying the functions of proteases, but this approach is hampered by the limited availability of inhibitor scaffold structures with the potential to allow rapid discovery of selective, noncovalent small-mol. protease inhibitors. The natural product class of Ahp cyclodepsipeptides is an unusual class of small-mol. canonical inhibitors; the incorporation of protease cleavage sequences into their mol. scaffolds enables the design of specific small-mol. inhibitors that simultaneously target the S and S’ subsites of the protease through noncovalent mechanisms. Their synthesis is tedious, however, so in this study we have investigated the relevance of the Ahp moiety for achieving potent inhibition. We found that although the Ahp residue plays an important role in inhibition potency, appropriate replacement with β-hydroxy amino acids results in structurally less complex derivatives that inhibit serine proteases in the low micromolar range.
ChemBioChem published new progress about 77128-73-5. 77128-73-5 belongs to ethers-buliding-blocks, auxiliary class Inhibitor, name is (S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)(methyl)amino)-3-phenylpropanoic acid, and the molecular formula is C12H12F3N5O2, Formula: C25H23NO4.
Referemce:
https://en.wikipedia.org/wiki/Ether,
Ether | (C2H5)2O – PubChem