PEGylated substrates of NSP4 protease: A tool to study protease specificity

Scientific Reports

Volumn 6, Issue , 2016, Pages

  Wysocka, Magdalena ^a   Gruba, Natalia ^a   Grzywa, Renata ^b   Giełdoń, Artur ^a   Bąchor, Remigiusz ^d   Brzozowski, Krzysztof ^a   Sieńczyk, Marcin ^b   Dieter, Jenne ^c   Szewczuk, Zbigniew ^d   Rolka, Krzysztof ^a   Lesner, Adam ^a  

^a UNIVERSITY OF GDA SK   (Poland)

^b WROCLAW UNIVERSITY OF TECHNOLOGY   (Poland)

^c INSTITUTE OF EPIDEMIOLOGY   (Germany)

^d UNIVERSITY OF WROC AW   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENT DYE; MYELOBLASTIN; PEPTIDOMIMETIC AGENT;

CHEMISTRY; DNA SEQUENCE; ENZYME SPECIFICITY; HUMAN; METABOLISM;

FLUORESCENT DYES; HUMANS; MYELOBLASTIN; PEPTIDOMIMETICS; SEQUENCE ANALYSIS, DNA; SUBSTRATE SPECIFICITY;

EID: 84960349715     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep22856     Document Type: Article

References (27)

1. Hu, H. Y. et al. FRET-based and other fluorescent proteinase probes. Biotechnol J. 9, 266-281 (2014).
2. Wysocka, M. & Lesner, A. Future of protease activity assays. Curr Pharm Des. 19, 1062-1067 (2013).
3. Korkmaz, B. et al. Design and use of highly specific substrates of neutrophil elastase and proteinase 3. Am J Respir Cell Mol Biol. 30, 801-807 (2004).
4. Schneider, E. L. & Craik, C. S. Positional scanning synthetic combinatorial libraries for substrate profiling. Methods Mol Biol. 539, 59-78 (2009).
5. Wysocka, M. et al. Substrate specificity and inhibitory study of human airway trypsin-like protease. Bioorg Med Chem. 18, 5504-5509 (2010).
6. Ziebuhr, J. et al. Human coronavirus 229E papain-like proteases have overlapping specificities but distinct functions in viral replication. J Virol. 81, 3922-3932 (2007).
7. Wysocka, M. et al. New chromogenic substrates of human neutrophil cathepsin G containing non-natural aromatic amino acid residues in position P(1) selected by combinatorial chemistry methods. Mol Divers. 11, 93-99 (2007).
8. Kasperkiewicz, P. et al. Design of ultrasensitive probes for human neutrophil elastase through hybrid combinatorial substrate library profiling. Proc Natl Acad Sci USA 111, 2518-2523 (2014).
9. Ginn, C., Khalili, H., Lever, R. & Brocchini, S. PEGylation and its impact on the design of new protein-based medicines. Future Med Chem. 6, 1829-1846 (2014).
10. Veronese, F. M. & Mero, A. The impact of PEGylation on biological therapies. BioDrugs. 22, 315-329 (2008).
11. Lesner, A. et al. Fluorescent analogs of trypsin inhibitor SFTI-1 isolated from sunflower seeds-synthesis and applications. Biopolymers. 102, 124-135 (2014).
12. Gokhale, S., Xu, Y. & Joy, A. A library of multifunctional polyesters with "peptide-like" pendant functional groups. Biomacromolecules. 14, 2489-2493 (2013).
13. Sadatmousavi, P., Mamo, T. & Chen, P. Diethylene glycol functionalized self-assembling peptide nanofibers and their hydrophobic drug delivery potential. Acta Biomater. 8, 3241-3250 (2012).
14. Veronese, F. Peptide and protein PEGylation: a review of problems and solutions. Biomaterials 22, 405-417 (2001).
15. Perera, N. C. et al. NSP4, an elastase-related protease in human neutrophils with arginine specificity. Proc Natl Acad Sci USA 109, 6229-6234 (2012).
16. Perera, N. C. et al. NSP4 is stored in azurophil granules and released by activated neutrophils as active endoprotease with restricted specificity. J Immunol. 191, 2700-2707 (2013).
17. Schechter, I. & Berger, A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162 (1967).
18. Lin, S. J., Dong, K. C., Eigenbrot, C., van Lookeren Campagne, M. & Kirchhofer, D. Structures of neutrophil serine protease 4 reveal an unusual mechanism of substrate recognition by a trypsin-fold protease. Structure. 22, 1333-1340 (2014).
19. Kasperkiewicz, P. et al. Design of a Selective Substrate and Activity Based Probe for Human Neutrophil Serine Protease 4. PLoS One. 10, e0132818 (2015).
20. Jabaiah, A. M., Getz, J. A., Witkowski, W. A., Hardy, J. A. & Daugherty, P. S. Identification of protease exosite-interacting peptides that enhance substrate cleavage kinetics. Biol Chem. 393, 162-167 (2012).
21. Lizama, A. J. et al. Expression and bioregulation of the kallikrein-related peptidases family in the human neutrophil. Innate Immun. (2015) Jan 6. In press.
22. Hojo, K. et al. Chem. Pharm. Bull. (Tokyo) 48, 1740-1744 (2000).
23. Bourel, L., Carion, O., Gras-Masse, H. & Melnyk, O. The deprotection of Lys(Mtt) revisited. J Pept Sci. 6, 264-270 (2000).
24. Sole, B. & Barany, G. Optimization of Solid-Phase Synthesis of. [Ala8]-dynorphin A. J. Org. Chem. 57, 5399-5403 (1992).
25. Houghten, R. A. et al. Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery. Nature 354, 84-86 (1991).
26. Wysocka, M. et al. Three wavelength substrate system of neutrophil serine proteinases. Anal. Chem. 84, 7241-7248 (2012).
27. Trott, O. & Olson, A. J. Auto Dock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem. 31, 455-461 (2010).