The first total synthesis of the cyclodepsipeptide pipecolidepsin A

Nature Communications

Volumn 4, Issue , 2013, Pages

  Pelay Gimeno, Marta ^a,b   García Ramos, Yésica ^a,b   Jesús Martin, Maria ^c   Spengler, Jan ^a,b   Molina Guijarro, José Manuel ^c   Munt, Simon ^c   Francesch, Andrés M ^c   Cuevas, Carmen ^c   Tulla Puche, Judit ^a,b   Albericio, Fernando ^a,b,d,e  

^a INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

^b BIOMATERIALES Y NANOMEDICINA CIBER BBN   (Spain)

^c PHARMAMAR S A   (Spain)

^d UNIVERSITY OF BARCELONA   (Spain)

^e UNIVERSITY OF KWAZULU NATAL   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; CYCLODEPSIPEPTIDE; HEXANOIC ACID DERIVATIVE; PIPECOLIDEPSIN A; UNCLASSIFIED DRUG;

AMINO ACID; BIOTECHNOLOGY; CANCER; CHEMICAL PROPERTY; CYTOLOGY; DISEASE TREATMENT; MARINE ENVIRONMENT; MEDICINE; PEPTIDE; SPONGE; TOXICITY;

ANTIPROLIFERATIVE ACTIVITY; ARTICLE; BIOLOGICAL ACTIVITY; CHEMICAL STRUCTURE; CYTOTOXICITY; IN VITRO STUDY; MOLECULE; PEPTIDE SYNTHESIS; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE; SOLID PHASE SYNTHESIS; STRUCTURE ACTIVITY RELATION;

ANIMALS; CELL LINE, TUMOR; DEPSIPEPTIDES; FEMALE; HEP G2 CELLS; HT29 CELLS; HUMANS; MALE; MCF-7 CELLS; NEOPLASMS; PIPECOLIC ACIDS; PORIFERA; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84884198777     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms3352     Document Type: Article

References (38)

1. Lemmens-Gruber, R., Kamyar, M. R. & Dornetshuber, R. Cyclodepsipeptides-potential drugs and lead compounds in the drug development process. Curr. Med. Chem. 16, 1122-1137 (2009).
2. Andavan, G. S. B. & Lemmens-Gruber, R. Cyclodepsipeptides from marine sponges: natural agents for drug research. Mar. Drugs 8, 810-834 (2010).
3. Suarez-Jimenez, G.-M., Burgos-Hernandez, A. & Ezquerra-Brauer, J.-M. Bioactive peptides and depsipeptides with anticancer potential: sources from marine animals. Mar. Drugs 10, 963-986 (2012).
4. Coello, L., Fernández, R., Reyes, J. F., Francesch, A. & Cuevas, M. D. C. Anticancer pipecolidepsins from marine organisms. Int. Appl. Pat. WO 2010/070078 A1, 24 June 2010.
5. Pelay-Gimeno, M., Tulla-Puche, J. & Albericio, F. 'Head-to-side-chain' cyclodepsipeptides of marine origin. Mar. Drugs 11, 1693-1717 (2013).
6. Zampella, A. et al. Callipeltin A, an anti-HIV cyclic depsipeptide from the new caledonian lithistida sponge Callipelta sp. J. Am. Chem. Soc. 118, 6202-6209 (1996). (Pubitemid 26236856)
7. Ford, P. W. et al. Papuamides A-D, HIV-inhibitory and cytotoxic depsipeptides from the sponges Theonella mirabilis and Theonella swinhoei collected in papua new guinea. J. Am. Chem. Soc. 121, 5899-5909 (1999). (Pubitemid 29305127)
8. Prasad, P., Aalbersberg, W., Feussner, K.-D. & Van Wagoner, R. M. Papuamides E and F, cytotoxic depsipeptides from the marine sponge Melophlus sp. Tetrahedron 67, 8529-8531 (2011).
9. Oku, N. et al. Neamphamide A, a new HIV-inhibitory depsipeptide from the papua new guinea marine sponge Neamphius huxleyi. J. Nat. Prod. 67, 1407-1411 (2004). (Pubitemid 39145653)
10. Yamano, Y., Arai, M. & Kobayashi, M. Neamphamide B, new cyclic depsipeptide, as an anti-dormant mycobacterial substance from a Japanese marine sponge of Neamphius sp. Bioorg. Med. Chem. Lett. 22, 4877-4881 (2012).
11. Tran, T. D. et al. Cytotoxic cyclic depsipeptides from the Australian marine sponge Neamphius huxleyi. J. Nat. Prod. 75, 2200-2208 (2012).
12. Ratnayake, A. S. et al. Theopapuamide, a cyclic depsipeptide from a papua new guinea lithistid sponge Theonella swinhoei. J. Nat. Prod. 69, 1582-1586 (2006). (Pubitemid 46031809)
13. Plaza, A. et al. Celebesides A-C and theopapuamides B-D, depsipeptides from an Indonesian sponge that inhibit HIV-1 entry. J. Org. Chem. 74, 504-512 (2009).
14. Plaza, A., Gustchina, E., Baker, H. L., Kelly, M. & Bewley, C. A. Mirabamides A-D, depsipeptides from the sponge Siliquariaspongia mirabilis that inhibit HIV-1 fusion. J. Nat. Prod. 70, 1753-1760 (2007). (Pubitemid 350275531)
15. Lu, Z. et al. Mirabamides E-H, HIV-inhibitory depsipeptides from the sponge Stelletta clavosa. J. Nat. Prod. 74, 185-193 (2011).
16. Zampella, A. et al. Homophymine A, an anti-HIV cyclodepsipeptide from the sponge Homophymia sp. J. Org. Chem. 73, 5319-5327 (2008).
17. Zampella, A. et al. Homophymines B-E and A1-E1, a family of bioactive cyclodepsipeptides from the sponge Homophymia sp. Org. Biomol. Chem. 7, 4037-4044 (2009).
18. Spengler, J., Pelay, M., Tulla-Puche, J. & Albericio, F. Synthesis of orthogonally protected L-threo-beta-ethoxyasparagine. Amino Acids 39, 161-165 (2010).
19. Çalimsiz, S., Morales Ramos, A. I. & Lipton, M. A. Solid-phase synthesis and configurational reassigment of callipeltin E. Implications for the structures of callipeltins A and B. J. Org. Chem. 71, 6351-6356 (2006). (Pubitemid 44252416)
20. Çalimsiz, S. & Lipton, M. A. Synthesis of N-Fmoc-(2S,3S,4R)-3, 4-dimethylglutamine: an application of lanthanide-catalyzed transamidation. J. Org. Chem. 70, 6218-6221 (2005). (Pubitemid 41076503)
21. Acevedo, C. M., Kogut, E. F. & Lipton, M. A. Synthesis and analysis of the sterically constrained l-glutamine l-pyroglutamic acid. Tetrahedron 57, 6353-6359 (2001).
22. Turk, J. A., Visbal, G. S. & Lipton, M. A. Asymmetric synthesis of four diastereomers of 3-hydroxy-2,4,6-trimethylheptanoic acid: proof of configurational assignment. J. Org. Chem. 68, 7841-7844 (2003).
23. Kolb, H. C., Vannieuwenhze, M. S. & Sharpless, K. B. Catalytic asymmetric dihydroxylation. Chem. Rev. 94, 2483-2547 (1994). (Pubitemid 24987874)
24. Wang, L. & Sharpless, K. B. Catalytic asymmetric dihydroxylation of cisdisubstituted olefins. J. Am. Chem. Soc. 114, 7568-7570 (1992).
25. Wang, Z.-M., Kakiuchi, K. & Sharpless, K. B. Osmium-catalyzed asymmetric dihydroxylation of cyclic cis-disubstituted olefins. J. Org. Chem. 59, 6895-6897 (1994).
26. Thoen, J. C., Morales-Ramos, A. I. & Lipton, M. A. Synthesis of the unnatural amino acid AGDHE, a constituent of the cyclic depsipeptides callipeltins A and D. Org. Lett. 4, 4455-4458 (2002).
27. Williams, L., Zhang, Z., Shao, F., Carroll, P. J. & Joulli, M. M. Grignard reactions to chiral oxazolidine aldehydes. Tetrahedron 52, 11673-11694 (1996). (Pubitemid 26280041)
28. Ohtaka, J., Hamajima, A., Nemoto, T. & Hamada, Y. Efficient diastereoselective synthesis of (2R,3R,4R)-2-amino-3-hydroxy-4,5- dimethylhexanoic acid, the lactone linkage unit of homophymine A. Chem. Pharm. Bull. 61, 245-250 (2013).
29. Albericio, F., Bofill, J. M., El-faham, A. & Kates, S. A. Use of onium salt-based coupling reagents in peptide synthesis 1. J. Org. Chem. 63, 9678-9683 (1998). (Pubitemid 29035117)
30. Boyd, M. R. & Paull, K. D. Some practical considerations and applications of the national cancer institute in vitro anticancer drug discovery screen. Drug Dev. Res. 34, 91-109 (1995).
31. Carpino, L. A., El-faham, A., Minorb, C. A. & Albericio, F. Advantageous applications of azabenzotriazole (triazo1opyridine)-based coupling reagents to solid-phase peptide synthesis. J. Chem. Soc., Chem. Commun. 201-203 (1994).
32. Barlos, K., Chatzi, O., Gatos, D. & Stavropoulos, G. 2-Chlorotrityl chloride resin: studies on anchoring of Fmoc-amino acids and peptide cleavage. Int. J. Pept. Prot. Res. 37, 513-520 (1991).
33. Barlos, K., Gatos, D., Kapolos, S., Poulos, W. S. & Wenqing, Y. Application of 2-chlorotrityl resin in solid phase synthesis of (Leu15)-gastrin I and unsulfated cholecystokinin octapeptide: Selective O-deprotection of tyrosine. Int. J. Pept. Prot. Res. 38, 555-561 (1991).
34. Wang, S.-S. p-Alkoxybenzyl alcohol resin and p- alkoxybenzyloxycarbonylhydrazide resin for solid phase synthesis of protected peptide fragments. J. Am. Chem. Soc. 95, 1328-1333 (1973).
35. Krishnamoorthy, R. et al. Solid-phase total synthesis and structure proof of callipeltin B. J. Am. Chem. Soc. 128, 15392-15393 (2006). (Pubitemid 44883035)
36. Tulla-Puche, J., Marcucci, E., Fermin, M., Bayó-Puxan, N. & Albericio, F. Protection by conformationally restricted mobility: first solid-phase synthesis of triostin A. Chem. Eur. J. 14, 4475-4478 (2008).
37. Molina-Guijarro, J. M. et al. Irvalec inserts into the plasma membrane causing rapid loss of integrity and necrotic cell death in tumor cells. PLoS One 6, e19042 (2011).
38. D'Auria, M. V. et al. Callipeltins B and C; bioactive peptides from a marine Lithistida sponge Callipelta sp. Tetrahedron 52, 9589-9596 (1996). (Pubitemid 26244576)