Solid-phase synthesis of the cyclic lipononadepsipeptide [N-Mst(Ser1), D-Ser4, L-Thr6, L-Asp8, L-Thr9]syringotoxin

Chemistry - A European Journal

Volumn 9, Issue 5, 2003, Pages 1096-1103

  Bayó, Nuria ^a   Jiménez, Jose C ^a   Rivas, Luis ^b   Nicolas, Ernesto ^a   Albericio, Fernando ^a  

^a UNIVERSITY OF BARCELONA   (Spain)

^b CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

Author keywords

Antimicrobial peptides; Cyclic peptides; Didehydroamino acids; Leishmania; Peptides; Protecting groups

Indexed keywords

SOLUBILITY; SYNTHESIS (CHEMICAL); WATER;

ORTHOGONAL PROTECTION SCHEME;

AMINO ACIDS;

AMINO ACID; ASPARTIC ACID; CYCLIC LIPONONADEPSIPEPTIDE; CYCLODEPSIPEPTIDE; DIPEPTIDE; HYDROXYL GROUP; IMIDE; SERINE; SYRINGOTOXIN; THREONINE; TOXIN; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL ANALYSIS; CHEMICAL REACTION; CHEMICAL STRUCTURE; DERIVATIZATION; SOLID STATE; STRUCTURE ACTIVITY RELATION; SYNTHESIS;

ANTI-INFECTIVE AGENTS; BACTERIAL TOXINS; COMBINATORIAL CHEMISTRY TECHNIQUES; PEPTIDES, CYCLIC;

EID: 0347294696     PISSN: 09476539     EISSN: None     Source Type: Journal    
DOI: 10.1002/chem.200390126     Document Type: Article

References (43)

1. C. L. Bender, F. Alarcón - Chaidez, D. C. Gros, Microbiol. Mol. Biol. Rev. 1999, 63, 266-292.
2. C. E. Ballard, H. Yu, B. Wang, Curr. Med. Chem. 2002, 9, 471-498.
3. A. M. Mayer, V. K. Lehmann. Anticancer Res. 2001, 21, 2489-2500.
4. Syringotoxin is a C-terminal to side chain heterodetic cyclic peptide as defined by: D. Andreu, F. Albericio, N. A. Solé, M. C. Munson, M. Ferrer, G. Barany, in Methods in Molecular Biology, Vol. 35: Peptide Synthesis Protocols (Eds.: M. W. Pennington, B. M. Dunn), Humana Press, Totowa, N. J., 1994, pp. 91-169.
5. P. Lavermicocca, N. Sante-Iacobellis, M. Simmaco, A. Graniti, Physiol. Mol. Plant Pathol. 1997, 50, 129-140.
6. R. Lozano, unpublished results.
7. B. L. Herwaldt, Lancet 1999, 354, 1191-1199.
8. P. Lloyd-Williams, F. Albericio, E. Giralt, Chemical Approaches to the Synthesis of Peptides and Proteins, CRC Press, Boca Raton (FL), 1997.
9. K. Barlos, D. Gatos, W. Schäfer, Angew. Chem. 1991, 103, 572-575; Angew. Chem. Int. Ed. Engl. 1991, 30, 590-593.
10. K. Barlos, D. Gatos, W. Schäfer, Angew. Chem. 1991, 103, 572-575; Angew. Chem. Int. Ed. Engl. 1991, 30, 590-593.
11. D. R. Bolin, I. Sytwu, F. Humiec, J. Meienhofer, Int. J. Peptide Protein Res. 1989, 33, 353-359.
12. F. Albericio, Biopolymers (Pept. Sci.) 2000, 55, 123-139.
13. M. Royo, J. C. Jiménez, A. López-Macià, E. Giralt, F. Albericio, Eur. J. Org. Chem. 2001, 45-48.
14. A. López-Macià, J. C. Jiménez, M. Royo, E. Giralt, F. Albericio, J. Am. Chem. Soc. 2001, 123, 11398-11401.
15. Fmoc-Thr(tBu)-OSu was prepared as was described in the experimental from the available amino acid Fmoc-Thr(tBu)-OH and HOSu (2 equiv) in the presence of DIPCDI (1.3 equiv). This reagent ratio was necessary to avoid formation of the inactive N-acylurea derivative of Fmoc-Thr(tBu)-OH.
16. Attempts to prepare Fmoc-Thr(tBu)-Thr-Oallyl from Fmoc-Thr(tBu)-OH and HCl·H-Thr-Oallyl by using carbodiimide-based methods (EDC·HCl/DIEA, DIPCDI/DIEA, DIPCDI/HOBt/DIEA) led to incomplete dipeptide formation, presumably due to some degree of steric hindrance between the two β-branched amino acids.
17. K. Fukase, M. Kitazawa, A. Sano, K. Shimbo, S. Horimoto, H. Fujita, A. Kubo, T. Wakamiya, A. Shibe, Bull. Chem. Soc. Jpn. 1992, 65, 2227-2240.
18. [12]), in this case a by-product (18%) was obtained that could be a cyclic compound with the carbodiimide serving as a bridge between the OH of the Thr and the C-carboxyl group. This result, which requires the replacement of the allyl group by EDC, was verified by the use of the phenacyl group as a carboxylic acid protecting group. In this case the acetophenone is a better leaving group and, consequently, a larger amount of the same by-product was obtained (35%).
19. N. Thieriet, J. Alsina, E. Giralt, F. Guibé, F. Albericio, Tetrahedron Lett. 1997, 38, 7275-7278.
20. [12] This result can be interpreted in terms of the steric hindrance between β-branched residues.
21. -1) for the preparation of hydrophobic peptides usually leads to impure peptides: C. Chiva, M. Vilaseca, E. Giralt, F. Albericio, J. Pept. Sci. 1999, 5, 131-140.
22. Unreacted reactive sites were capped with MeOH/DIEA.
23. DKP formation is favored by the presence of Gly.
24. a) O. Kuisle, E. Quiñoá, R. Riguera, J. Org. Chem. 1999, 64, 8063-8075:
25. b) S. K. Latypov, J. M. Seco, E. Quiñoá, R. Riguera, J. Am. Chem. Soc. 1998, 120, 877-882:
26. c) A. Hassner, V. Alexanian, Tetrahedron Lett. 1978, 46, 4475-4478.
27. O. Kuisle, M. Lolo, E. Quifioa, R. Riguera, Tetrahedron 1999, 55, 14807-14812.
28. L. A. Carpino, J. Am. Chem. Soc. 1993, 115, 4397-4398.
29. As the activation of the carboxyl function is more demanding in this case, the use of the most reactive amidium salts, such as N-[(dimethylamino)-1H-1,2,3-triazolo-[4,5-b]pyridin-1-yl-methylene]- N-methylmethanaminium hexafluorophosphate N-oxide (HATU), is not recommended because HATU can react with the free amino function of the amino acid bound to the resin. This produces a guanidinium species with concomitant termination of the peptide: M. del Fresno. A. El-Faham, L.A. Carpino, M. Royo, F. Albericio, Organic Lett. 2000, 2, 3539-3542, and references therein.
30. The use of other scavengers, such as morpholine or N-methylmorpholine/HOAc, leads to back alkylation of the allyl carbocation: P. Gómez-Martínez, M. Dessolin, F. Guibé, F. Albericio. J. Chem. Soc. Perkin Trans. 1 1999, 2871-2874.
31. The presence of DIEA avoids the trifluoroacetylation of the free amine function.
32. M. Carrascal. J. C. Jiménez, E. Giralt, F. Albericio, unpublished results.
33. H. Lackner, I. Bahner, N. Shigematsu, L. K. Pannell, A. B. Mauger, J. Nat. Prod. 2000, 63, 352-356.
34. H. Uemoto, Y. Yahiro, H. Shigemori, M. Tsuda, T. Takao, Y. Shimonishi, J. Kobayashi, Tetrahedron 1998, 54, 6719-6724.
35. A. E. Shinnar, T. Uzzel, M. N. Rao, R. E. Spooner, W. S. Lane, M. A. Zasloff, in Peptides: Chemistry, Structure and Biology (Eds.: P. T. P. Kaumaya, R. S. Hodges), Mayflower Scientific Ltd., Kingswinford, UK, 1996, pp. 189-191.
36. S. W. Taylor, A. G. Craig, W. H. Fischer, H. Park, R. I. Lehrer, J. Biol Chem. 2000, 275, 38417-38426.
37. I. Grgurina, A. Barca, S. Cervigni, M. Gallo, A. Scaloni, P. Pucci, Experientia 1994, 50, 130-133.
38. C. Chicharro, C. Granata, R. Lozano, D. Andreu, L. Rivas, Antimicrob. Agents. Chemother. 2001, 45, 2441-2449.
39. H. Wakabayashi, H. Matsumoto, K. Hashimoto, S, Teraguchi, M. Takase, H. Hayasawa, Agents Chemother. 1999, 43, 1267-1269.
40. K. Hemmi, C. Julmanop, D. Hirata, E. Tsuchiya, J. Y. Takemoto, T. Miyakawa, Biosci. Biotechnol. Biochem. 1995, 159, 482-486.
41. H. Hama, D. A. Young, J. A. Radding, D. Ma, J. Tang, S. D. Stock, J. Y. Takemoto. FEBS Lett. 2000, 478, 26-28.
42. M. Trabi, D. J. Craik, Trends Biochem. Sci. 2002, 27, 132-138.
43. S. C. Ilgoutz, M. J. McConville, Int. J Parasitol. 2001, 31, 899-908.