Peptide substrates for determination of protease activity

Details Peptide substrates for determination of protease activity Peptide substrates for determination of protease activity

1987-05-21

1988-05-31

Phillips, Delbert R.

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving hydrolase

530330, 530331, 530802, C12Q 138, C07K 506, C07K 508, C07K 510

Patent

active

047481161

ABSTRACT:
Peptide sequences consisting of 2-4 amino acids with high affinity and comparatively high specificity to a number of various, physiologically important proteases are known to have been synthetized before. Such sequences with an added C-terminal marker have been widely used as substrates for the quantitative determination of the kind of proteases mentioned above. The method is based on the fact that the marker is split off under influence of the enzyme and that the liberated marker possesses an easily measurable, for instance, optic property which differs from that of the original substrate. The type of markers used until today have mainly been chromophores or fluorophores which can be quantified by photometry or fluorometry.
The present invention relates to a new type of markers coupled to known peptide sequences. These markers are luminol or isoluminol which in their free state can be brought to luminate intensely, but lose considerably in luminescence when they are amide-bound to a peptide sequence.
The peptide derivatives consist of acyl derivates of luminol (5-amino-2,3-dihydro-1,4-phthalazinedione) or isoluminol (6-amino-2,3-dihydro-1,4-phthalazinedione) where the acyl residue consists of an amide-bound amino acid or amino acid sequence with 2-4 amino acid residues and where the .alpha.-amino group is either free of acylated.
The greatest advantages of the luminogenic substrates according to the invention are that they

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