Synthetic substrate for high specificity enzymatic assays

Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S007720, C435S023000, C435S174000

Reexamination Certificate

active

10233908

ABSTRACT:
Novel synthetic enzyme substrates, enhanced to have improved enzymatic specificity, are disclosed. These synthetic enzyme substrates consist of a substrate peptide that has had its specificity further improved by additional synthetic moieties, selected by combinatorial chemistry techniques, that act to sterically block non-target enzymes. These “steric restrictor” moieties may be labeled to produce a detectable signal upon enzymatic reaction. These novel substrates are particularly useful for improved enzyme substrate microarrays. Specific applications for improved protease substrate microarrays are discussed. A variety of applications for these improved protease substrate microarrays are also disclosed, including proteomics research, protease discovery, protease binding site characterization, diagnosis of the protease composition of biological samples, monitoring the angiogenic status of a tumor, monitoring the status of arthritis and other inflammatory diseases, and the discovery and optimization of novel drugs that modify or inhibit protease activity.

REFERENCES:
patent: 4247454 (1981-01-01), af Ekenstam et al.
patent: 4557862 (1985-12-01), Mangel et al.
patent: 4897444 (1990-01-01), Brynes et al.
patent: 5413854 (1995-05-01), Sato
patent: 5418143 (1995-05-01), Zweig
patent: 5580747 (1996-12-01), Shultz et al.
patent: 5605809 (1997-02-01), Komoriya et al.
patent: 5741659 (1998-04-01), Ralls et al.
patent: 6037137 (2000-03-01), Komoriya et al.
patent: 6248904 (2001-06-01), Zhang et al.
patent: 2003/0186345 (2003-10-01), Hortin
Tung et al. “In vivo imaging of proteolytic enzyme activity using a novel molecular reporter,” J. Cancer Res. (Sep. 2000) 60: 49534958.
Benacerraf et al. “Artificial antigens. II. The antigenicity in guinea pigs of arsanilic acid conjugates of copolymers of D- or L-alpha-amino acids,” J. Experimental Med. (1963) 118(6): 945-952.
Hugues et al. “Conjugation of methotrexate to Poly(L-lysine) as a potential way to overcome drug resistance” Cancer (1980) 54: 1207-1211.
Anjuere et al. “Sensitive, hydrosoluble, macromolecular fluoregenic substrates for human immunodeficiency virus 1 proteinase,” Biochem. J. (1993) 291: 869-873.
King, t. “Immunological properties of protein conjugates with non-immunogenic polymers: Studies wit ragweed pollen allergen, antigen E.” Versitility Proteins, [Proc. Int. Symp. Proteins] Ed: Li, D. (Academic: New York, NY) (1978) 335-351.
Liu et al. “New procedures for preparation and isolation of conjugates of proteins and a synthetic copolymer of D-Amino Acids and immunochemical characterization of such conjugates” Biochemistry (1979) 18(4):690-697.
Harris et. al., Proc. Natl. Acad. Sciences (2000); 97(14), 7754-7759.
Lam and Lebl, Methods Mol. Biol. (1998); 87: 1-6.
Folkman et. al., Thromb. Haemost (2001); 86: 23-33.
Knight, Methods in Enzymology (1995); 248: 18-34.
Groutas, et. al., Bioorg Med. Chem. (2001); Jun. 9(6): 1543-1548.
Fodor et. al., Science (1991); 251: 767-773.
MacBeath and Schreiber, Science (2001); 289: 1760-1763.
Turk, et. al., Nature Biotechnology (2001); 19: 661-677.
Lebl and Krchnak, Methods in Enzymology (1997); 289: 336-392.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Synthetic substrate for high specificity enzymatic assays does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Synthetic substrate for high specificity enzymatic assays, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Synthetic substrate for high specificity enzymatic assays will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3816643

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.