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  • 1
    Electronic Resource
    Electronic Resource
    Specificity of Cathepsin B to Fluorescent Substrates Containing Benzyl Side-Chain-Substituted Amino Acids at P1 Subsite (2000)
    Springer
    The protein journal 19 (2000), S. 33-38 
    Details
    ISSN: 1573-4943
    Keywords: Thiolprotease ; cathepsins B ; papain ; fluorogenic substrate ; fluorescent peptides ; proteinases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract We have determined the kinetic parameters for the hydrolysis by cathepsin B of peptidyl-coumarin amide and intramolecularly quenched fluorogenic peptides with the general structures εNH2-Cap-Leu-X-MCA and Abz-Lys-Leu-X-Phe-Ser-Lys-Gln-EDDnp, respectively. Abz (ortho-aminobenzoic acid) and EDDnp (2,4-dinitrophenyl-ethylenediamine) are the fluorescent donor-acceptor pair, and X was Cys(SBzl), Ser(OBzl), and Thr(OBzl) containing benzyl group (Bzl) at the functional side chain of Cys, Ser, and Thr. The peptidyl-coumarin-containing Cys(SBzl), Ser(OBzl), and Thr(OBzl) have higher affinity cathepsin B, supporting the interpretation of the crystal structure of rat cathepsin B complexed with the inhibitor Z-Arg-Ser(OBzl)-CH2Cl that the benzyl group attached to Ser hydroxyl side chain occupies the enzyme S′1 subsite [Jia et al. (1995), J. Biol. Chem. 270, 5527]. A similar effect of benzyl group was also detected in the internally quenched peptides. Finally, the benzyl group in substrates containing Cys(SBzl) amino acid at P1 seems to compensate the absence of adequate S2-P2 interaction in the hydrolysis of the peptides having Pro or Ala at P2 position.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007090708945
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  • 2
    Electronic Resource
    Electronic Resource
    Inhibition of cruzipain visualized in a fluorescence quenched solid-phase inhibitor library assay. D-Amino Acid Inhibitors for cruzipain, cathepsin B and cathepsin L (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 83-91 
    Details
    ISSN: 1075-2617
    Keywords: fluorescence quenched assay ; inhibitor library ; Trypanosoma cruzi ; cathepsin B and L inhibitors ; Parasitic protease inhibition ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A PEGA-resin was derivatized with a 3:1 mixture of hydroxymethyl benzoic acid and Fmoc-Lys(Boc)-OH and the fluorogenic substrate Ac-Y(NO2)KLRFSKQK(Abz)-PEGA was assembled on the lysine using the active ester approach. Following esterification of the hydroxymethyl benzoic acid with Fmoc-Val-OH a library XXX-k/r-XXXV containing approximately 200,000 beads was assembled by split synthesis. The resulting ‘one bead, two peptides’ library was subjected to extensive hydrolysis with cruzipain. One hundred darker beads were isolated and the 14 most persistently dark beads were collected and sequenced. The putative inhibitor peptides and several analogues were synthesized and found to be competitive μM to nM inhibitors of cruzipain in solution. The inhibitory activity was found to be unspecific to cruzipain when compared with cathepsins B and L and specific when compared with kallikrein. One of the inhibitors was docked into the active site of the cathepsin B and was found most probably to bind to the enzyme cavity in an unusual manner, owing to the inserted D-amino acid residue. © 1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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