A study of aspartyl proteases using intramolecularly quenched fluorogenic peptide substrates

被引:0
|
作者
Filippova, IY [1 ]
Lysogorskaya, EN [1 ]
Lavrenova, GI [1 ]
Oksenoit, ES [1 ]
Suvorov, LI [1 ]
Starovoitova, VV [1 ]
机构
[1] Moscow MV Lomonosov State Univ, Fac Chem, Moscow 119899, Russia
来源
BIOORGANICHESKAYA KHIMIYA | 2000年 / 26卷 / 03期
关键词
aspartyl proteases; fluorogenic peptide substrates;
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学科分类号
摘要
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.
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页码:192 / 196
页数:5
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