Serum stable natural peptides designed by mRNA display

Scientific Reports

Volumn 4, Issue , 2014, Pages

  Howell, Shannon M ^a   Fiacco, Stephen V ^a   Takahashi, Terry T ^a   Jalali Yazdi, Farzad ^b   Millward, Steven W ^c   Hu, Biliang ^b   Wang, Pin ^b   Roberts, Richard W ^a,b  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^b University of Southern California   (United States)

^c UNIVERSITY OF TEXAS MD ANDERSON CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PEPTIDE; PEPTIDE HYDROLASE; PEPTIDE LIBRARY; PLASMA PROTEIN; PROTEIN BINDING;

AMINO ACID SEQUENCE; CHEMISTRY; GENETICS; HUMAN; PEPTIDE LIBRARY; PROTEIN DEGRADATION;

AMINO ACID SEQUENCE; BLOOD PROTEINS; HUMANS; PEPTIDE HYDROLASES; PEPTIDE LIBRARY; PEPTIDES; PROTEIN BINDING; PROTEOLYSIS; RNA, MESSENGER;

EID: 84923344557     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep06008     Document Type: Article

References (25)

1. McGregor, D. P. Discovering and improving novel peptide therapeutics. Curr. Opin. Pharmacol. 8, 616-619 (2008).
2. Donzel, B., Goodman, M., Rivier, J., Ling, N. & Vale, W. Synthesis and conformations of hypothalamic hormone releasing factors: two QRF-analogues containing backbone N-methyl groups. Nature 256, 750-751 (1975).
3. Dado, G. P. & Gellman, S. H. Intramolecular Hydrogen-Bonding in Derivatives of Beta-Alanine and Gamma-Amino Butyric-Acid-Model Studies for the Folding of Unnatural Polypeptide Backbones. J. Am. Chem. Soc. 116, 1054-1062 (1994).
4. Seebach, D. & Matthews, J. L. beta-peptides: a surprise at every turn. Chem. Commun. 2015-2022 (1997).
5. Owens, R. A., Gesellchen, P. D., Houchins, B. J. & DiMarchi, R. D. The rapid identification of HIV protease inhibitors through the synthesis and screening of defined peptide mixtures. Biochem. Biophys. Res. Commun. 181, 402-408 (1991).
6. Simon, R. J. et al. Peptoids: A modular approach to drug discovery. Proc. Natl. Acad. Sci. USA 89, 9367-9371 (1992).
7. Blackwell, H. E. et al. Ring-closing metathesis of olefinic peptides: Design, synthesis, and structural characterization of macrocyclic helical peptides. J. Org. Chem. 66, 5291-5301 (2001).
8. Walensky, L. D. et al. Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix. Science 305, 1466-1470 (2004).
9. Roberts, R. W. & Szostak, J. W. RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. USA 94, 12297-12302 (1997).
10. Millward, S. W., Takahashi, T. T. & Roberts, R. W. A General Route for Post-Translational Cyclization of mRNA Display Libraries. J. Am. Chem. Soc. 127, 14142-14143 (2005).
11. Millward, S. W., Fiacco, S., Austin, R. J. & Roberts, R. W. Design of Cyclic Peptides that Bind Protein Surfaces with Antibody-Like Affinity. ACS Chem. Biol. 2, 625-634 (2007).
12. Hedstrom, L., Szilagyi, L. & Rutter, W. J. Converting trypsin to chymotrypsin: the role of surface loops. Science 255, 1249-1253 (1992).
13. Austin, R. J., Ja, W. W. & Roberts, R. W. Evolution of class-specific peptides targeting a hot spot of the Gas subunit. J. Mol. Biol. 377, 1406-1418 (2008).
14. Ja, W. W. & Roberts, R. W. In vitro selection of state-specific peptide modulators of G protein signaling using mRNA display. Biochemistry 43, 9265-9275 (2004).
15. Johnston, C. A. et al. Structure of Galpha(i1) bound to a GDP-selective peptide provides insight into guanine nucleotide exchange. Structure (Camb) 13, 1069-1080 (2005).
16. Folk, J. E. & Cole, P. W. Chymotrypsin C. Ii. Enzymatic Specificity toward Several Polypeptides. J. Biol. Chem. 240, 193-197 (1965).
17. Schellenberger, V., Braune, K., Hofmann, H. J. & Jakubke, H. D. The specificity of chymotrypsin. A statistical analysis of hydrolysis data. Eur. J. Biochem./FEBS 199, 623-636 (1991).
18. Hedstrom, L. Serine protease mechanism and specificity. Chem. Rev. 102, 4501-4524 (2002).
19. Fung, B. K. & Nash, C. R. Characterization of transducin from bovine retinal rod outer segments. II. Evidence for distinct binding sites and conformational changes revealed by limited proteolysis with trypsin. J. Biol. Chem. 258, 10503-10510 (1983).
20. Hurley, J. B., Simon, M. I., Teplow, D. B., Robishaw, J. D. & Gilman, A. G. Homologies between signal transducingGproteins and ras gene products. Science 226, 860-862 (1984).
21. Marqusee, S. & Baldwin, R. L. Helix stabilization by Glu2?Lys1 salt bridges in short peptides of de novo design. P. Natl. Acad. Sci. USA 84, 8898-8902 (1987).
22. Marqusee, S., Robbins, V. H. & Baldwin, R. L. Unusually stable helix formation in short alanine-based peptides. P. Natl. Acad. Sci. USA 86, 5286-5290 (1989).
23. Compton, L. A. & Johnson, W. C., Jr. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155, 155-167 (1986).
24. Powell, M. F. et al. Peptide stability in drug development. II. Effect of single amino acid substitution and glycosylation on peptide reactivity in human serum. Pharm. Res. 10, 1268-1273 (1993).
25. Wildes, D. & Wells, J. A. Sampling the N-terminal proteome of human blood. P. Natl. Acad. Sci. USA 107, 4561-4566 (2010).