Iterative optimization of high-affinity protease inhibitors using phage display. 1. Plasmin

Biochemistry

Volumn 35, Issue 24, 1996, Pages 8045-8057

  Markland, William ^a,b   Ley, Arthur Charles ^a   Lee, Stanley W ^a   Ladner, Robert Charles ^a  

^a Protein Engineering Corporation   (United States)

^b VERTEX PHARMACEUTICALS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APROTININ; BINDING PROTEIN; PLASMIN; PROTEINASE INHIBITOR; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; THROMBOPLASTIN; TISSUE FACTOR PATHWAY INHIBITOR;

AMINO ACID SEQUENCE; ARTICLE; BACTERIOPHAGE; FIBRINOLYSIS; GENE LIBRARY; GENETIC ENGINEERING; HEMOSTASIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN ISOLATION; PROTEIN MODIFICATION; PROTEIN POLYMORPHISM; PROTEIN STABILITY;

AMINO ACID SEQUENCE; APROTININ; BACTERIOPHAGE M13; BASE SEQUENCE; GENE LIBRARY; HUMANS; LIPOPROTEINS; MODELS, STRUCTURAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, INSERTIONAL; PLASMIN; PROTEIN STRUCTURE, SECONDARY; RESTRICTION MAPPING; SEQUENCE HOMOLOGY, AMINO ACID; SERINE PROTEINASE INHIBITORS; THROMBIN; VARIATION (GENETICS);

EID: 0029953760     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9526286     Document Type: Article

References (34)

1. 561-Plasmin: A Comparative Study, Biochim. Biophys. Acta 1040, 134-136.
2. 52] Aprotinin, Biol. Chem. Hoppe-Seyler 369 (Suppl.), 27-35.
3. Barr, K. A., Hopkins, S. A., & Sreekrishna, K. (1992) Protocol for Efficient Secretion of HSA Developed from Pichia pastoris, Pharm. Eng. 12, 48-51.
4. Bieth, J. G. (1984) In vivo Significance of Kinetic Constants of Protein Proteinase Inhibitors, Biochem. Med. 32, 387-397.
5. Clackson, T., & Wells, J. A. (1994) In vitro Selection from Protein and Peptide Libraries, Trends Biotechnol. 12, 173-184.
6. Clackson, T., & Wells, J. A. (1995) A Hot Spot of Binding Energy in a Hormone-Receptor Interface, Science 267, 383-386.
7. Colman, R. W., Hirsh, J., Marder, V. J., & Salzman, E. W., Eds. (1987) Hemostasis and Thrombosis, 2nd ed., J. B. Lippincott Company, Philadelphia, PA.
8. Concetti, A., Angeletti, M., Fioretti, E., & Ascoli, F. (1988) Selective Oxidation of Methionine Residues in Kunitz-Type Protease Inhibitors, Biol. Chem. Hoppe-Seyler 370, 723-728.
9. a. I. Potent Inhibitors Selected from Libraries by Phage Display, J. Biol. Chem. 269, 22129-22136.
10. a. II. Potent and Specific Inhibitors by Competitive Phage Section, J. Biol. Chem. 269, 22137-22144.
11. Fritz, H., & Wunderer, G. (1983) Biochemistry and Applications of Aprotinin: The Kallikrein Inhibitor from Bovine Organs, Arzneim.-Forsch. 33, 479-494.
12. Girard, T. J., Warren, L. A., Novotny, W. F., Likert, K. M., Brown, S. G., Miletich, J. P., & Broze, G. J. (1989) Functional Significance of the Kunitz-Type Domains of Lipoprotein-Associated Coagulation Inhibitor, Nature 338, 518-520.
13. Hynes, T. R., Randal, M., Kennedy, L. A., Eigenbrot, C., & Kossiakoff, A. A. (1990) X-ray Crystal Structure of the Protease Inhibitor Domain of Alzheimer's Amyloid β-Protein Precursor, Biochemistry 29, 10018-10022.
14. Kido, H., Fukutomi, A., Schilling, J., Wang, Y., Cordell, B., & Katunuma, N. (1990) Protease-Specificity of Kunitz Inhibitor Domain of Alzheimer's Disease Amyloid Protein Precursor, Biochem. Biophys. Res. Commun. 167, 716-721.
15. Ladner, R. C. (1996) in Phage Display of Peptides and Protein Domains: A Laboratory Manual, (Kay, B., Winter, J., & McCafferty, J., Eds.) Chapter 10, Academic Press, San Diego, CA.
16. Ladner, R. C., & Guterman, S. K. (1990) Directed Evolution of Novel Binding Proteins, Pat. Appl. WO90/02809.
17. McLafferty, M. A., Kent, R. B., Ladner, R. C., & Markland, W. (1993) M13 Bacteriophage Displaying Disulfide-Constrained Microproteins, Gene 128, 29-36.
18. Markland, W., Roberts, B. L., Saxena, M. J., Guterman, S. K., & Ladner, R. C. (1991) Design, Construction and Function'of a Multicopy Display Vector Using Fusions to the Major Coat Protein of Bacteriophage M13, Gene 109, 13-19.
19. Markland, W., Roberts, B. L., & Ladner, R. C. (1996) Selection for Protease Inhibitors Using Bacteriophage Display, Methods Enzymol. 263, 28-51.
20. Miyajima, A., Bond, M. W., Otsu, K., Arai, K.-I., & Arai, N. (1985) Secretion of Mature Mouse Interleukin-2 by Saccharomyces cerevisiae: Use of a General Secretion Vector Containing Promoter and Leader Sequences of the Mating Pheromone α Factor, Gene 37, 155-161.
21. Robbins, K. C. (1987) in Hemostasis and Thrombosis, 2nd ed., (Colman, R. W., Hirsh, J., Marder, V. J., & Salzman, E. W., Eds.) J. B. Lippincott Company, Philadelphia, PA.
22. Roberts, B. L., Markland, W., Ley, A. C., Kent, R. B., White, D. W., Guterman, S. K., & Ladner, R. C. (1992a) Directed Evolution of a Protein: Selection of Potent Neutrophil Elastase Inhibitors Displayed on M13 Fusion Phage, Proc. Natl. Acad. Sci. U.S.A. 89, 2429-2433.
23. Roberts, B. L., Markland, W., Siranosian, K., Saxena, M. J., Guterman, S. K., & Ladner, R. C. (1992b) Protease Inhibitor Display M13 Phage: Selection of High Affinity Neutrophil Elastase Inhibitors, Gene 121, 9-15.
24. Schechter, K., & Berger, A. (1968) On the Active Site of Proteases. III. Mapping the Active Site of Papain; Specific Peptide Inhibitors of Papain, Biochem. Biophys. Res. Commun. 32, 898-902.
25. Schnabel, E., Reinhardt, G., Schroeder, W., Tschesche, H., Wenzel, H. R., & Mehlich, A. (1988) Enzymatic Resynthesis of the "Reactive Site" Bond in the Modified Aprotinin Derivatives [Seco-15/16]Aprotinin and [Di-seco-15/16,39/40]Aprotinin, Biol. Chem. Hoppe-Seyler 369, 461-468.
26. Scott, C. F., Wenzel, H. R., Tschesche, H. R., & Colman, R. W. (1987) Kinetics of Inhibition of Human Plasma Kallikrein by a Site-Specific Modified Inhibitor Arg15-Aprotinin: Evaluation Using a Microplate System and Comparison with Other Proteases, Blood 69, 1431-1436.
27. Smith, G. P., & Scott, J. K. (1993) Libraries of Peptides and Proteins Displayed on Filamentous Phage, Methods Enzymol. 217, 228-257.
28. Stoll, V. S., & Blanchard, J. S. (1990) Buffers: Principles and Practice, Methods Enzymol. 182, 24-38.
29. Szardenings, M., Vasel, B., Hecht, H.-J., Collins, J., & Schomburg, D. (1995) Highly Effective Protease Inhibitors from Variants of Human Pancreatic Secretory Trypsin Inhibitor (hPSTI): An Assessment of 3-D Structure-Based Protein Design, Protein Eng. 8, 45-52.
30. Vedvick, T., Buckholtz, R. G., Engel, M., Urcam, M., Kinney, S., Provow, S., Siegel, R. S., & Thill, G. P. (1991) High Level Secretion of Biologically Active Aprotinin from the Yeast Pichia pastoris, J. Ind. Microbiol. 7, 197-202.
31. Verstraete, M. (1985) Clinical Application of Inhibitors of Fibrinolysis, Drugs 29, 236-261.
32. Wagner, S. L., Siegel, R. S., Vedvick, T. S., Raschke, W. C., & Van Nostrand. W. E. (1992) High Level Expression, Purification, and Characterization of the Kunitz-Type Protease Inhibitor Domain of Protease Nexin-2/Amyloid β-Protein Precursor, Biochem. Biophys. Res. Commun. 186, 1138-1145.
33. Wells, J. A. (1990) Additivity of Mutational Effects in Proteins, Biochemistry 29, 8509-8517.
34. 2-Antiplasmin, Thromb. Res. 17, 143-152.