@article{ref1,
title="Cyclopeptidic inactivators for chymotrypsin-like proteinases",
journal="European journal of medicinal chemistry",
year="1991",
author="Wakselman, M. and Mazaleyrat, J. and Xie, J. and Montagne, J. and Vilain, A. and Reboud-Ravaux, M.",
volume="26",
number="7",
pages="699-707",
abstract="Cyclopeptides containing a functionalized meta-aminobenzoic acid residue (m-aB[CH2X] with X = OC6H5, OAc, Br, C1) linked to a tetraglycyl-phenylalanyl sequence, have been synthesized in solution. A phenyl ether group has been used during chain elongation and cyclisation, and then cleaved by treatment with HBr/HOAc to give the corresponding bromide, from which the acetate and the chloride have been obtained. The functionalized aminobenzoic acid residues possess a latent quinonimmonium methide electrophilic function, and these cyclopeptides are potential &quot;suicide&quot; substrates of chymotrypsin-like proteases. The cyclopeptides with X = Br or Cl irreversibly inhibit α-chymotrypsin ( kinact KI = 180 M-1min-1 for X = Cl). The compounds with poorer leaving groups X = OAc or OC6H5 are devoid of inactivating effect and only behave as substrates of this enzyme ( kcat KM = 31 800 M-1min-1 and 120 000 M-1min-1, respectively). © 1991.<p /><p>Language: en</p>",
language="en",
issn="0223-5234",
doi="10.1016/0223-5234(91)90119-8",
url="http://dx.doi.org/10.1016/0223-5234(91)90119-8"
}