[A study of aspartyl proteases using intramolecularly quenched fluorogenic peptide substrates].
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.
Filippova
I Iu
IIu
Moscow State University, Chemical Faculty, GSP Moscow, Russia. irfilipp@genebee.msu.su
Lysogorskaia
E N
EN
Lavrenova
G I
GI
Oksenoĭt
E S
ES
Suvorov
L I
LI
Starovoĭtova
V V
VV
D016282:Aspartic Acid Endopeptidases / Q000032:analysis* / Q000737:chemistry*; D005453:Fluorescence; D006801:Humans; D010455:Peptides / Q000737:chemistry*; D013379:Substrate Specificity
D010455:Peptides; D016282:Aspartic Acid Endopeptidases