title: [A study of aspartyl proteases using intramolecularly quenched fluorogenic peptide substrates].
abstract: A series of fluorogenic tetra-, penta-, and hexapeptide substrates of the general structure Abz-X-Phe-Phe-Y-Ded (or -pNa in place of -Ded), where X = Ala, Ala-Ala, or Val-Ala and Y = -, Ala, or Ala-Ala, were proposed. Kinetic parameters of hydrolysis of these substrates by pepsin, cathepsin D, human gastricsin, pig pepsin, calf chymosin, and aspergillopepsin A were determined. The compounds synthesized proved to be effective substrates for aspartyl proteases of diverse origins.
authors.affiliation: Moscow State University, Chemical Faculty, GSP Moscow, Russia. irfilipp@genebee.msu.su
authors.forename: I Iu
authors.initials: IIu
authors.lastname: Filippova
authors.forename: E N
authors.initials: EN
authors.lastname: Lysogorskaia
authors.forename: G I
authors.initials: GI
authors.lastname: Lavrenova
authors.forename: E S
authors.initials: ES
authors.lastname: Oksenoĭt
authors.forename: L I
authors.initials: LI
authors.lastname: Suvorov
authors.forename: V V
authors.initials: VV
authors.lastname: Starovoĭtova
mesh_terms: D016282:Aspartic Acid Endopeptidases / Q000032:analysis* / Q000737:chemistry*; D005453:Fluorescence; D006801:Humans; D010455:Peptides / Q000737:chemistry*; D013379:Substrate Specificity
chemical_list: D010455:Peptides; D016282:Aspartic Acid Endopeptidases