Synthesis of anticancer heptapeptides containing a unique lipophilic β 2,2-amino acid building block

Journal of Peptide Science

Volumn 18, Issue 3, 2012, Pages 170-176

  Tørfoss, Veronika ^a   Ausbacher, Dominik ^a   Cavalcanti Jacobsen, Cristiane de A ^a   Hansen, Terkel ^a   Brandsdal, Bjørn Olav ^b   Havelkova, Martina ^a   Strøm, Morten B ^a  

^a UNIVERSITY OF TROMSØ   (Norway)

^b Faculty of Science and Technology   (Norway)

Author keywords

2,2 amino acids; Anticancer peptides; Heptapeptides; Peptide synthesis

Indexed keywords

ANTINEOPLASTIC AGENT; BETA AMINO ACID; HEPTAPEPTIDE;

ANIMAL CELL; ANTINEOPLASTIC ACTIVITY; ARTICLE; B CELL LYMPHOMA; BURKITT LYMPHOMA; CONTROLLED STUDY; DRUG CYTOTOXICITY; DRUG POTENCY; DRUG STABILITY; DRUG SYNTHESIS; HUMAN; HUMAN CELL; IC 50; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; TOXICITY TESTING;

AMINO ACIDS; ANIMALS; ANTINEOPLASTIC AGENTS; BURKITT LYMPHOMA; CELL LINE, TUMOR; HUMANS; INHIBITORY CONCENTRATION 50; LEUKOCYTES, MONONUCLEAR; LYMPHOMA, B-CELL; MICE; OLIGOPEPTIDES;

MURINAE;

EID: 84857508171     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1434     Document Type: Article

References (32)

1. Smith L. L., Brown K., Carthew P., Lim C.-K., Martin E. A., Styles J., White I. N. H. Chemoprevention of breast cancer by tamoxifen: risks and opportunities. Crit. Rev. Toxicol. 2000; 30: 571-594. DOI: 10.1080/10408440008951120
2. Gerber D. E. Targeted therapies: a new generation of cancer treatments. Am. Fam. Physician 2008; 77: 311-319.
3. Pérez-Tomás R. Multidrug resistance: retrospect and prospects in anti-cancer drug treatment. Curr. Med. Chem. 2006; 13: 1859-1876.
4. Ellis L. M., Hicklin D. J. Resistance to targeted therapies: refining anticancer therapy in the era of molecular oncology. Clin. Cancer Res. 2009; 15: 7471-7478.
5. Mader J. S., Hoskin D. W. Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment. Expert Opin. Investig. Drugs 2006; 15: 933-946.
6. Hoskin D. W., Ramamoorthy, A. Studies on anticancer activities of antimicrobial peptides. BBA - Biomembranes 2008; 1778: 357-375.
7. Eliassen L. T., Berge G., Leknessund A., Wikman M., Lindin I., Løkke C., Ponthan F., Johnsen J. I., Sveinbjørnsson B., Kogner P., Flægstad T., Rekdal Ø. The antimicrobial peptide, lactoferricin B, is cytotoxic to neuroblastoma cells in vitro and inhibits xenograft growth in vivo. Int. J. Cancer 2006; 119: 493-500.
8. Kim S., Kim S. S., Bang Y. J., Kim S. J., Lee B. J. In vitro activities of native and designed peptide antibiotics against drug sensitive and resistant tumor cell lines. Peptides 2003; 24: 945-953.
9. Berge G., Eliassen L., Camilio K., Bartnes K., Sveinbjørnsson B., Rekdal Ø. Therapeutic vaccination against a murine lymphoma by intratumoral injection of a cationic anticancer peptide. Cancer Immunol. Immun. 2010; 59: 1285-1294. DOI: 10.1007/s00262-010-0857-6
10. Papo N., Shai Y. Host defense peptides as new weapons in cancer treatment. Cell. Mol. Life Sci. 2005; 62: 784-790.
11. Fuster M. M., Esko J. D. The sweet and sour of cancer: glycans as novel therapeutic targets. Nat. Rev. Cancer 2005; 5: 526-542.
12. Leuschner C., Hansel W. Membrane disrupting lytic peptides for cancer treatments. Curr. Pharm. Design 2004; 10: 2299-2310.
13. Richardson A., de Antueno R., Duncan R., Hoskin D. W. Intracellular delivery of bovine lactoferricin's antimicrobial core (RRWQWR) kills T-leukemia cells. Biochem. Bioph. Res. Co. 2009; 388: 736-741.
14. Schibli D. J., Hwang P. M., Vogel H. J. The structure of the antimicrobial active center of lactoferricin B bound to sodium dodecyl sulfate micelles. FEBS Lett. 1999; 446: 213-217.
15. Hansen T., Alst T., Havelkova M., Strøm M. B. Antimicrobial activity of small β-Peptidomimetics based on the pharmacophore model of short cationic antimicrobial peptides. J. Med. Chem. 2010; 53: 595-606. DOI:10.1021/jm901052r
16. 2, 2-amino acid derivatives with potential for oral administration. J. Med. Chem. 2011; 54: 858-868. 10.1021/jm101327d
17. 3, 3-amino acids: A turn motif for β-peptides. Helv. Chim. Acta 1998; 81: 2218-2243.
18. 3, 3-amino acids at the central position. Amino Acids 2006; 30: 453-459.
19. Yang S.-T., Shin S. Y., Lee C. W., Kim Y.-C., Hahm K.-S., Kim J. I. Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure. FEBS Lett. 2003; 540: 229-233. DOI: 10.1016/s0014-5793(03)00266-7
20. Gottlieb H. E., Kotlyar V., Nudelman A. NMR chemical shifts of common laboratory solvents as trace impurities. J. Org. Chem. 1997; 62: 7512-7515.
21. Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 1983; 65: 55-63.
22. Eliassen L. T., Berge G., Svinbjørnsson B., Svendsen J. S., Vorland L. H., Rekdal Ø. Evidence for a direct antitumor mechanism of action of bovine lactoferricin. Anticancer Res 2002; 22: 2703-2710.
23. Svenson J., Karstad R., Flaten G. E., Brandsdal B.-O., Brandl M. Svendsen J. S. Altered activity and physicochemical properties of short cationic antimicrobial peptides by incorporation of arginine analogues. Mol. Pharmaceutics 2009; 6: 996-1005. DOI: 10.1021/mp900057k
24. Cronin J. R., Yuen G. U., Pizzarello S. Gas chromatographic-mass spectral analysis of the five-carbon β-, γ- and δ-amino alkanoic acids. Anal. Biochem. 1982; 124: 139-149.
25. Bodanszky M., Bodanszky A. The Practice of Peptide Synthesis. 2nd ed, Berlin Heidelberg: Springer-Verlag, 1994.
26. Iwasaki T., Ishibashi J., Tanaka H., Sato M., Asaoka A., Taylor D. Yamakawa M. Selective cancer cell cytotoxicity of enantiomeric 9-mer peptides derived from beetle defensins depends on negatively charged phosphatidylserine on the cell surface. Peptides 2009; 30: 660-668.
27. Hagmann W. K. The many roles for fluorine in medicinal chemistry. J. Med. Chem. 2008; 51: 4359-4369. DOI: 10.1021/jm800219f
28. Giménez D., Andreu C., Olmo M. d., Varea T., Diaz D., Asensio G. The introduction of fluorine atoms or trifluoromethyl groups in short cationic peptides enhances their antimicrobial activity. Bioorgan. Med. Chem. 2006; 14: 6971-6978.
29. Amin K., Dannenfelser R. M. In vitro hemolysis: guidance for the pharmaceutical scientist. J. Pharm. Sci. 2006; 95: 1173-1176. 10.1002/jps.20627
30. Adessi C., Soto C. Converting a peptide into a drug: strategies to improve stability and bioavailability. Curr. Med. Chem. 2002; 9: 963-978.
31. Frackenpohl J., Arvidsson P. I., Schreiber J. V., Seebach D. The outstanding biological stability of β- and γ-peptides toward proteolytic enzymes: an in vitro investigation with fifteen peptidases. Chembiochem 2001; 2: 445-455.
32. 3-2-methylidene-amino acids bearing proteinogenic side chains - A survey. Chem. Biodiversity 2005; 2: 401-420.