Natural Cyclopeptides: Comparison
Please note this is a comparison between Version 2 by Camila Xu and Version 1 by Hongjie Zhang.

The present review mainly focuses on the anticancer efficacies, mechanisms of action and chemical structures of 236 cyclopeptides with natural origins. Additionally, studies of the structure–activity relationship, total synthetic strategies as well as bioactivities of natural cyclopeptides are also included in this article. Herein, we provide an overview of anticancer cyclopeptides that were discovered in the past 20 years. Full contents of the review report can be found in International Journal of Molecular Sciences 2021, 22(8), 3973; https://doi.org/10.3390/ijms22083973.

Cyclopeptides, also known as cyclic peptides, are polypeptides formed from amino acids arranged in a cyclic ring structure.

  • cyclopeptides
  • anticancer
  • natural products
Please wait, diff process is still running!

References

  1. Torre, L.A.; Bray, F.; Siegel, R.L.; Ferlay, J.; Lortet-tieulent, J.; Jemal, A. Global Cancer Statistics, 2012, CA a Cancer. J. Clin. 2015, 65, 87–108.
  2. Bray, F.; Ferlay, J.; Soerjomataram, I.; Siegel, R.L.; Torre, L.A.; Jemal, A. Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J. Clin. 2018, 68, 394–424.
  3. American Cancer Society. Global Cancer Facts & Figures 4th Edition. Atlanta: American Cancer Society. 2018. Available online: (accessed on 12 April 2021).
  4. Appold, K. Cancer Treatment—Top 4 Developments to Watch. 2017. Available online: (accessed on 12 April 2021).
  5. Kang, T.H.; Mao, C.P.; He, L.; Tsai, Y.C.; Liu, K.; La, V.; Wu, T.C.; Hung, C.F. Tumor-targeted delivery of IL-2 by NKG2D leads to accumulation of antigen-specific CD8+ T cells in the tumor loci and enhanced anti-tumor effects. PLoS ONE 2012, 7, e35141.
  6. Amit, D.; Tamir, S.; Hochberg, A. Development of targeted therapy for a broad spectrum of solid tumors mediated by a double promoter plasmid expressing diphtheria toxin under the control of IGF2-P4 and IGF2-P3 regulatory sequences. Int. J. Clin. Exp. Med. 2013, 6, 110–118.
  7. Peer, D.; Karp, J.M.; Hong, S.; Farokhzad, O.C.; Margalit, R.; Langer, R. Nanocarriers as an emerging platform for cancer therapy. Nat. NanoTechnol. 2007, 2, 751–760.
  8. Pawar, S.V.; Ho, J.C.H.; Yadav, G.D.; Yadav, V.G. The impending renaissance in discovery & development of natural products. Curr. Top. Med. Chem. 2017, 251–267.
  9. Butler, M.S. The role of natural product chemistry in drug discovery. J. Nat. Prod. 2004, 67, 2141–2153.
  10. Joo, S.H. Cyclic peptides as therapeutic agents and biochemical tools. Biomol. Ther. 2012, 20, 19–26.
  11. Wipf, P. Synthetic studies of biologically active marine cyclopeptides. Chem. Rev. 1995, 95, 2115–2134.
  12. Pomilio, A.; Battista, M.; Vitale, A. Naturally-occurring cyclopeptides: Structures and bioactivity. Curr. Org. Chem. 2006, 10, 2075–2121.
  13. Tran, D.; Selsted, M.E.; Dorrestein, P.C.; Pavel, A. Cycloquest: Identification of cyclopeptides via database search of their mass spectra against genome databases. NIH Public Access. 2012, 10, 4505–4512.
  14. Tan, N.H.; Zhou, J. Plant cyclopeptides. Chem. Rev. 2006, 106, 840–895.
  15. Marahiel, M.A.; Stachelhaus, T.; Mootz, H.D. Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem. Rev. 1997, 97, 2651–2674.
  16. Hur, G.H.; Vickery, C.R.; Burkart, M.D. Explorations of catalytic domains in non-ribosomal peptide synthetase enzymology. Nat. Prod. Rep. 2012, 29, 1074–1098.
  17. Salomon, R.A.; Farias, R.N. Microcin 25, a novel antimicrobial peptide produced by Escherichia coli. J. Bacteriol. 1992.
  18. Luckett, S.; Garcia, R.S.; Barker, J.J.; Konarev, A.V.; Shewry, P.R.; Clarke, A.R.; Brady, R.L. High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds. J. Mol. Biol. 1999, 290, 525–533.
  19. Tang, Y.Q.; Yuan, J.; Ösapay, G.; Ösapay, K.; Tran, D.; Miller, C.J.; Ouellette, A.J.; Selsted, M.E. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins. Science 1999, 286, 498–502.
  20. Closse, A.; Huguenin, R. Isolierung und Strukturaufklärung von Chlamydocin. Helv. Chim. Acta 1974, 57, 533–545.
  21. Mollica, A.; Costante, R.; Stefanucci, A.; Novellino, E. Cyclotides: A natural combinatorial peptide library or a bioactive sequence player? J. Enzym. Inhib. Med. Chem. 2015, 30, 575–580.
  22. Edman, P. Chemistry of amino acids and peptides. Annu. Rev. Biochem. 1959, 28, 69–96.
  23. Trabi, M.; Craik, D.J. Circular proteins-No end in sight. Trends Biochem. Sci. 2002, 27, 132–138.
  24. Rezai, T.; Yu, B.; Millhauser, G.L.; Jacobson, M.P.; Lokey, R.S. Testing the conformational hypothesis of passive membrane permeability using synthetic cyclic peptide diastereomers. J. Am. Chem. Soc. 2006, 128, 2510–2511.
  25. Áron, R. Towards Targeted Photodynamic Therapy: Synthesis and Characterization of Aziridine Aldehyde-Cyclized Cancer-Targeting Peptides and Bacteriochlorin Photosensitizers. Ph.D. Thesis, University of Toronto, Toronto, ON, Canada, 2014.
  26. Malaker, A.; Ahmad, S.A.I. Therapeutic potency of anticancer peptides derived from marine organism. Int. J. Eng. Appl. Sci. 2013, 2, 53–65.
  27. Liu, J.; Gu, B.; Yang, L.; Yang, F.; Lin, H.; Yang, F. New anti-inflammatory cyclopeptides from a sponge-derived fungus Aspergillus violaceofuscus. Front. Chem. 2018, 6, 1–8.
  28. Desriac, F.; Jé, C.; Balnois, E.; Brillet, B.; le Chevalier, P. Antimicrobial peptides from marine proteobacteria. Mar. Drugs 2013, 11, 3632–3660.
  29. Wu, W.; Zhen, Z.; Niu, T.; Zhu, X.; Gao, Y.; Yan, J.; Chen, Y.; Yan, X.; Chen, H. κ-Carrageenan enhances lipopolysaccharide-induced interleukin-8 secretion by stimulating the Bcl10-NF-κB pathway in HT-29 cells and aggravates C. freundii-Induced inflammation in mice. Mediat. Inflamm. 2017, 2017, 8634865.
  30. Randazzo, A.; Bifulco, G.; Giannini, C.; Bucci, M.; Cirino, G.; Gomez-paloma, L.; Ponte, V.; Salerno, F.; Ii, F.; Montesano, V.D.; et al. Halipeptins A and B: Two novel potent anti-inflammatory cyclic depsipeptides from the Vanuatu marine sponge Haliclona species. J. Am. Chem. Soc. 2001, 123, 10870–10876.
  31. Xing, H.; Tong, M.; Jiang, N.; Zhang, X.; Hu, H.; Pan, H.; Li, D. Antitumour bioactive peptides isolated from marine organisms. Clin. Exp. Pharmacol. Physiol. 2017, 44, 1077–1082.
  32. Laport, M.; Santos, O.; Muricy, G. Marine sponges: Potential sources of new antimicrobial drugs. Curr. Pharm. BioTechnol. 2009, 10, 86–105.
  33. Mehbub, M.F.; Lei, J.; Franco, C.; Zhang, W. Marine Sponge derived natural products between 2001 and 2010: Trends and opportunities for discovery of bioactives. Mar. Drugs 2014, 12, 4539–4577.
  34. Kang, H.K.; Choi, M.C.; Seo, C.H.; Park, Y. Therapeutic properties and biological benefits of marine-derived anticancer peptides. Int. J. Mol. Sci. 2018, 19, 919.
  35. Nakao, Y.; Yoshida, S.; Matsunaga, S.; Shindoh, N.; Terada, Y.; Nagai, K.; Yamashita, J.K.; Ganesan, A.; van Soest, R.W.M.; Fusetani, N. Azumamides A-E: Histone deacetylase inhibitory cyclic tetrapeptides from the marine sponge Mycale izuensis. Angew. Chem. Int. Ed. 2006, 45, 7553–7557.
  36. Sriraksa, R.; Limpaiboon, T. Histone deacetylases and their inhibitors as potential therapeutic drugs for cholangiocarcinoma-cell line findings. Asian Pac. J. Cancer Prev. 2013, 14, 2503–2508.
  37. Abdalla, M.A. Medicinal significance of naturally occurring cyclotetrapeptides. J. Nat. Med. 2016, 70, 708–720.
  38. Maulucci, N.; Chini, M.G.; di Micco, S.; Izzo, I.; Cafaro, E.; Russo, A.; Gallinari, P.; Paolini, C.; Nardi, M.C.; Casapullo, A.; et al. Molecular insights into azumamide E histone deacetylases inhibitory activity. J. Am. Chem. Soc. 2007, 129, 3007–3012.
  39. Wen, S.; Carey, K.L.; Nakao, Y.; Fusetani, N.; Packham, G.; Ganesan, A. Total synthesis of azumamide A and azumamide E, evaluation as histone deacetylase inhibitors, and design of a more potent analogue. Org. Lett. 2007, 9, 1105–1108.
  40. Zhang, X.; Jacob, M.R.; Rao, R.R.; Wang, Y.H.; Agarwal, A.K.; Newman, D.J.; Khan, I.A.; Clark, A.M.; Li, X.C. Antifungal cyclic peptides from the marine sponge Microscleroderma herdmani [Corrigendum]. Res. Rep. Med. Chem. 2013, 3, 9–10.
  41. Bewley, C.A.; Detritus, C.; Faulkner, D.J. Microsclerodermins A and B. Antifungal cyclic peptides from the lithistid sponge Microscleroderma sp. J. Am. Chem. Soc. 1994, 116, 7631–7636.
  42. Guzmán, E.A.; Maers, K.; Roberts, J.; Kemami-Wangun, H.V.; Harmody, D.; Wright, A.E. The marine natural product microsclerodermin A is a novel inhibitor of the nuclear factor kappa B and induces apoptosis in pancreatic cancer cells. Investig. New Drugs. 2015, 33, 86–94.
  43. Kehraus, S.; Ko, G.M.; Wright, A.D.; Bonn, D.; Woerheide, G.; Reef, B. Leucamide A: A new cytotoxic heptapeptide from the Australian sponge Leucetta microraphis leucamide. J. Org. Chem. 2002, 67, 4989–4992.
  44. Wang, W.; Nan, F. First total synthesis of leucamide A. J. Org. Chem. 2003, 68, 1636–1639.
  45. Afifi, A.H.; El-Desoky, A.H.; Kato, H.; Mangindaan, R.E.P.; de Voogd, N.J.; Ammar, N.M.; Hifnawy, M.S.; Tsukamoto, S. Carteritins A and B, cyclic heptapeptides from the marine sponge Stylissa carteri. Tetrahedron Lett. 2016, 57, 1285–1288.
  46. Sun, J.; Cheng, W.; de Voogd, N.J.; Proksch, P.; Lin, W. Stylissatins B–D, cycloheptapeptides from the marine sponge Stylissa massa. Tetrahedron Lett. 2016, 57, 4288–4292.
  47. Bonnington, L.S.; Tanaka, J.; Higa, T.; Kimura, J.; Yoshimura, Y.; Nakao, Y.; Yoshida, W.Y.; Scheuer, P.J. Cupolamide A: A cytotoxic cyclic heptapeptide from two samples of the sponge Theonella cupola. J. Org. Chem. 2002, 62, 7765–7767.
  48. Rangel, M.; Konno, K.; Brunaldi, K.; Procopio, J.; de Freitas, J.C. Neurotoxic activity induced by a haemolytic substance in the extract of the marine sponge Geodia corticostylifera. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2005, 141, 207–215.
  49. Rangel, M.; Prado, M.P.; Konno, K.; Naoki, H.; Freitas, J.C.; Machado-Santelli, G.M. Cytoskeleton alterations induced by Geodia corticostylifera depsipeptides in breast cancer cells. Peptides 2006, 27, 2047–2057.
  50. Freitas, V.M.; Rangel, M.; Bisson, L.F.; Jaeger, R.G.; Machado-Santelli, G.M. The geodiamolide H, derived from Brazilian sponge Geodia corticostylifera, regulates actin cytoskeleton, migration and invasion of breast cancer cells cultured in three-dimensional environment. J. Cell. Physiol. 2008, 216, 583–594.
  51. Ratnayake, A.S.; Bugni, T.S.; Feng, X.; Harper, M.K.; Skalicky, J.J.; Mohammed, K.A.; Andjelic, C.D.; Barrows, L.R.; Ireland, C.M. Theopapuamide, a cyclic depsipeptide from a Papua New Guinea lithistid sponge Theonella swinhoei. J. Nat. Prod. 2006, 69, 1582–1586.
  52. Zampella, A.; Sepe, V.; Bellotta, F.; Luciano, P.; D’Auria, M.V.; Cresteil, T.; Debitus, C.; Petek, S.; Poupat, C.; Ahond, A. Homophymines B-E and A1-E1, a family of bioactive cyclodepsipeptides from the sponge Homophymia sp. Org. Biomol. Chem. 2009, 7, 4037–4044.
  53. Zampella, A.; Sepe, V.; Luciano, P.; Bellotta, F.; Monti, M.C.; D’Auria, M.V.; Jepsen, T.; Petek, S.; Adeline, M.T.; Laprévôte, O.; et al. Homophymine A, an anti-HIV cyclodepsipeptide from the sponge Homophymia sp. J. Org. Chem. 2008, 73, 5319–5327.
  54. Sorres, J.; Martin, M.T.; Petek, S.; Levaique, H.; Cresteil, T.; Ramos, S.; Thoison, O.; Debitus, C.; Al-Mourabit, A. Pipestelides A–C: Cyclodepsipeptides from the pacific marine sponge Pipestela candelabra. J. Nat. Prod. 2012, 75, 759–763.
  55. Tran, T.D.; Pham, N.B.; Fechner, G.; Zencak, D.; Vu, H.T.; Hooper, J.N.A.; Quinn, R.J. Cytotoxic cyclic depsipeptides from the Australian marine sponge Neamphius huxleyi. J. Nat. Prod. 2012, 75, 2200–2208.
  56. 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. Bioorganic Med. Chem. Lett. 2012, 22, 4877–4881.
  57. Stierhof, M.; Hansen, K.Ø.; Sharma, M.; Feussner, K.; Subko, K.; Díaz-Rullo, F.F.; Isaksson, J.; Pérez-Victoria, I.; Clarke, D.; Hansen, E.; et al. New cytotoxic callipeltins from the Solomon Island marine sponge Asteropus sp. Tetrahedron 2016, 72, 6929–6934.
  58. Coello, L.; Reyes, F.; Martín, M.J.; Cuevas, C.; Fernández, R. Isolation and structures of pipecolidepsins A and B, cytotoxic cyclic depsipeptides from the madagascan sponge Homophymia lamellosa. J. Nat. Prod. 2014, 77, 298–303.
  59. Gimeno, M.P. Synthesis, Structural Elucidation and Biological Evaluation of Pipecolidepsin A and Synthesis, Structural Elucidation and Biological Evaluation of Pipecolidepsin A and Phakellistatin 19. Ph.D. Thesis, University of Barcelona, Barcelona, Spain, 2013.
  60. Molina-Guijarro, J.M.; Moneo, V.; Martinez-Leal, J.F.; Cuevas, C.; Garcia-Fernandez, L.F.; Galmarini, C.M. Pipecolidepsin A, stellatolide A and irvalec: New cyclodepsipeptides of marine origin with antitumor activity. Eur. J. Cancer 2014, 50, 24.
  61. Pelay-Gimeno, M.; García-Ramos, Y.; Martin, M.J.; Spengler, J.; Molina-Guijarro, J.M.; Munt, S.; Francesch, A.M.; Cuevas, C.; Tulla-Puche, J.; Albericio, F. The first total synthesis of the cyclodepsipeptide pipecolidepsin A. Nat. Commun. 2013, 4, 1–10.
  62. Nicolaou, K.C.; Schlawe, D.; Kim, D.W.; Longbottom, D.A.; de Noronha, R.G.; Lizos, D.E.; Manam, R.R.; Faulkner, D.J. Total synthesis of halipeptins: Isolation of halipeptin D and synthesis of oxazoline halipeptin analogues. Chem. A Eur. J. 2005, 11, 6198–6211.
  63. Nicolaou, K.C.; Lizos, D.E.; Kim, D.W.; Schlawe, D.; de Noronha, R.G.; Longbottom, D.A.; Rodriquez, M.; Bucci, M.; Cirino, G. Total synthesis and biological evaluation of halipeptins A and D and analogues. J. Am. Chem. Soc. 2006, 128, 4460–4470.
  64. Zhan, K.; Jiao, W.; Yang, F.; Li, J.; Wang, S.; Li, Y.; Han, B.; Lin, H. Reniochalistatins A−E, cyclic peptides from the marine sponge Reniochalina stalagmitis. J. Nat. Prod. 2014, 77, 2678–2684.
  65. Fatino, A.; Baca, G.; Weeramange, C.; Rafferty, R.J. Total synthesis of reniochalistatin E. J. Nat. Prod. 2017, 80, 3234–3240.
  66. Ibrahim, S.R.M.; Edrada-Ebel, R.A.; Mohamed, G.A.; Youssef, D.T.A.; Wray, V.; Proksch, P. Callyaerin G, a new cytotoxic cyclic peptide from the marine sponge Callyspongia aerizusa. Arkivoc 2008, 12, 164–171.
  67. Ibrahim, S.R.M.; Min, C.C.; Teuscher, F.; Ebel, R.; Kakoschke, C.; Lin, W.; Wray, V.; Edrada-Ebel, R.; Proksch, P. Callyaerins A-F and H, new cytotoxic cyclic peptides from the Indonesian marine sponge Callyspongia aerizusa. Bioorganic Med. Chem. 2010, 18, 4947–4956.
  68. Schmidt, E.W.; Raventos-Suarez, C.; Bifano, M.; Menendez, A.T.; Fairchild, C.R.; Faulkner, D.J. Scleritodermin A, a cytotoxic cyclic peptide from the Lithistid sponge Scleritoderma nodosum. J. Nat. Prod. 2004, 67, 475–478.
  69. Sellanes, D.; Manta, E.; Serra, G. Toward the total synthesis of Scleritodermin A: Preparation of the C1-N15 fragment. Tetrahedron Lett. 2007, 48, 1827–1830.
  70. Liu, S.; Cui, Y.M.; Nan, F.J. Total synthesis of the originally proposed and revised structures of scleritodermin A. Org. Lett. 2008, 10, 3765–3768.
  71. Kimura, M.; Wakimoto, T.; Egami, Y.; Tan, K.C.; Ise, Y.; Abe, I. Calyxamides A and B, cytotoxic cyclic peptides from the marine sponge Discodermia calyx. J. Nat. Prod. 2012, 75, 290–294.
  72. Kobayashi, J.; Itagaki, F.; Shigemori, I.; Takao, T.; Shimonishi, Y. Keramamides E, G, H, and J, new cyclic peptides containing an oxazole or a thiazole ring from a Theonella sponge. Tetrahedron 1995, 51, 2525–2532.
  73. Uemoto, H.; Yahiro, Y.; Shigemori, H.; Tsuda, M.; Takao, T.; Shimonishi, Y.; Kobayashi, J. Keramamides K and L, new cyclic peptides containing unusual tryptophan residue from Theonella sponge. Tetrahedron 1998, 54, 6719–6724.
  74. Tsuda, M.; Ishiyama, H.; Masuko, K.; Takao, T.; Shimonishi, Y.; Kobayashi, J. Keramamides M and N, two new cyclic peptides with a sulfate ester from Theonella sponge. Tetrahedron 1999, 55, 12543–12548.
  75. Junk, L.; Kazmaier, U. Total Synthesis of Keramamides A and L from a common precursor by late-stage indole synthesis and configurational revision. Angew. Chem. Int. Ed. 2018, 57, 11432–11435.
  76. Randazzo, A.; Dal, F.; Orru, S.; Gomez-paloma, L. Axinellins A and B: New proline-containing antiproliferative cyclopeptides from the Vanuatu sponge Axinella carteri. Eur. J. Org. Chem. 1998, 3, 2659–2665.
  77. Fairweather, K.A.; Sayyadi, N.; Roussakis, C.; Jolliffe, K.A. Synthesis of the cyclic heptapeptide axinellin A. Tetrahedron 2010, 66, 935–939.
  78. Brennan, M.R.; Costello, C.E.; Maleknia, S.D.; Pettit, G.R.; Erickson, K.L. Stylopeptide 2, a proline-rich cyclodecapeptide from the sponge Stylotella sp. J. Nat. Prod. 2008, 71, 453–456.
  79. Arai, M.; Yamano, Y.; Fujita, M.; Setiawan, A.; Kobayashi, M. Stylissamide X, a new proline-rich cyclic octapeptide as an inhibitor of cell migration, from an Indonesian marine sponge of Stylissa sp. Bioorganic Med. Chem. Lett. 2012, 22, 1818–1821.
  80. Huang, T.; Zou, Y.; Wu, M.C.; Zhao, Q.J.; Hu, H.G. Total synthesis of proline-rich cyclic octapeptide stylissamide X. Chem. Nat. Compd. 2015, 51, 523–526.
  81. Bewley, C.A.; He, H.; Williams, D.H.; Faulkner, D.J. Aciculitins A–C: Cytotoxic and antifungal cyclic peptides from the lithistid sponge Aciculites orientalis. J. Am. Chem. Soc. 1996, 118, 4314–4321.
  82. Fukuhara, K.; Takada, K.; Okada, S.; Matsunaga, S. Nazumazoles A-C, cyclic pentapeptides dimerized through a disulfide bond from the marine sponge Theonella swinhoei. Org. Lett. 2015, 17, 2646–2648.
  83. Youssef, D.T.A.; Shaala, L.A.; Mohamed, G.A.; Badr, J.M.; Bamanie, F.H.; Ibrahim, S.R.M. Theonellamide G, a potent antifungal and cytotoxic bicyclic glycopeptide from the red sea marine sponge Theonella swinhoei. Mar. Drugs 2014, 12, 1911–1923.
  84. Araki, T.; Matsunaga, S.; Nakao, Y.; Furihata, K.; West, L.; Faulkner, D.J.; Fusetani, N. Koshikamide B, a cytotoxic peptide lactone from a marine sponge Theonella sp. J. Org. Chem. 2008, 73, 7889–7894.
  85. Shenkar, N.; Swalla, B.J. Global diversity of Ascidiacea. PLoS ONE 2011, 6, e20657.
  86. Marino, A.; Rajendran, N.M. Natural products diversity of marine ascidians (Tunicates; Ascidiacea) and successful drugs in clinical development. Nat. Prod. Bioprospect 2017, 7, 1–111.
  87. Hockless, D.C.R.; Skelton, B.W.; White, A.H. Studies of australian ascidians. IV. mollamide, a cytotoxic cyclic heptapeptide from the compound ascidian. Aust. J. Chem. 1994, 47, 61–69.
  88. McKeever, B.; Pattenden, G. Total synthesis of the cytotoxic cyclopeptide mollamide, isolated from the sea squirt Didemnum molle. Tetrahedron 2003, 59, 2701–2712.
  89. Donia, M.S.; Wang, B.; Dunbar, D.C.; Desai, P.V.; Patny, A.; Avery, M.; Hamann, M.T. Mollamides B and C, cyclic hexapeptides from the indonesian tunicate Didemnum molle. J. Nat. Prod. 2008, 71, 941–945.
  90. McKeever, B.; Pattenden, G. Total synthesis of trunkamide A, a novel thiazoline-based prenylated cyclopeptide metabolite from Lissoclinum sp. Tetrahedron 2003, 59, 2713–2727.
  91. Bowden, B.F.; Garcia, G.D. A Cyclic Hepta-Peptide Derivative from Colonial Ascidians, Lissoclinum sp. European Patent EP0894092B1, 3 April 2002.
  92. Fu, X.; Su, J.; Zeng, L. Prepatellamide A, a new cyclic peptide from the ascidian Lissoclinum patella. Sci. China Ser. B Chem. 2008, 43, 643–648.
  93. Fernandez, A.M. Isolation and Characterization of Vitilevuamide from the Ascidians Didemnum cuculliferum and Polysyncraton lithostrotum. Ph.D. Thesis, The University of Utah, Salt Lake City, UT, USA, 1996.
  94. Edler, M.C.; Fernandez, A.M.; Lassota, P.; Ireland, C.M.; Barrows, L.R. Inhibition of tubulin polymerization by vitilevuamide, a bicyclic marine peptide, at a site distinct from colchicine, the vinca alkaloids, and dolastatin 10. Biochem. Pharmacol. 2002, 63, 707–715.
  95. Pangestuti, R.; Kim, S.K. Bioactive peptide of marine origin for the prevention and treatment of non-communicable diseases. Mar. Drugs 2017, 15, 67.
  96. Vervoort, H.; Fenical, W.; Epifanio, R.D.A. Tamandarins A and B: New cytotoxic depsipeptides from a Brazilian ascidian of the family Didemnidae. J. Org. Chem. 2000, 65, 782–792.
  97. Liang, B.; Richard, D.J.; Portonovo, P.S.; Joullie, M.M. Total Syntheses and biological investigations of tamandarins A and B and tamandarin A analogs. J. Am. Chem. Soc. 2001, 123, 4469–4474.
  98. Rudi, A.; Aknin, M.; Gaydou, E.M.; Kashman, Y. Four new cytotoxic cyclic hexa- and heptapeptides from the marine ascidian Didemnum molle. Tetrahedron 1998, 54, 13203–13210.
  99. Carroll, A.; Coll, J.; Bourne, D.; Macleod, J.; Zabriskie, T.; Ireland, C.; Bowden, B. Patellins 1–6 and trunkamide A: Novel cyclic hexa-, hepta- and octa-peptides from colonial ascidians, Lissoclinum sp. Aust. J. Chem. 1996, 49, 659–667.
  100. Tan, K.C.; Wakimoto, T.; Takada, K.; Ohtsuki, T.; Uchiyama, N.; Goda, Y.; Abe, I. Cycloforskamide, a cytotoxic macrocyclic peptide from the sea slug Pleurobranchus forskalii. J. Nat. Prod. 2013, 76, 1388–1391.
  101. Rosenberg, G. A New critical estimate of named species-level diversity of the recent Mollusca. Am. Malacol. Bull. 2014, 32, 308–322.
  102. Chakraborty, S.; Ghosh, U. Oceans: A store house of drugs-a review. J. Pharm. Res. 2010, 3, 1293–1296.
  103. Wesson, K.J.; Hamann, M.T. Keenamide A, a bioactive cyclic peptide from the marine mollusk Pleurobranchus forskalii. J. Nat. Prod. 1996, 59, 629–631.
  104. Suenaga, K.; Mutou, T.; Shibata, T.; Itoh, T.; Fujita, T.; Takada, N.; Hayamizu, K.; Takagi, M.; Irifune, T. Aurilide, a cytotoxic depsipeptide from the sea hare Dolabella auricularia: Isolation, structure determination, synthesis, and biological activity. Tetrahedron 2004, 60, 8509–8527.
  105. Sato, S.I.; Murata, A.; Orihara, T.; Shirakawa, T.; Suenaga, K.; Kigoshi, H.; Uesugi, M. Marine natural product aurilide activates the opa1-mediated apoptosis by binding to prohibitin. Chem. Biol. 2011, 18, 131–139.
  106. Pettit, G.R.; Xu, J.P.; Hogan, F.; Williams, M.D.; Doubek, D.L.; Schmidt, J.M.; Cerny, R.L.; Boyd, M.R. Isolation and structure of the human cancer cell growth inhibitory cyclodepsipeptide dolastatin 16. J. Nat. Prod. 1997, 60, 752–754.
  107. Ishiwata, H.; Nemoto, T.; Ojika, M.; Yamada, K. Isolation and stereostructure of doliculide, a cytotoxic cyclodepsipeptide from the Japanese sea hare Dolabella auricularia. J. Org. Chem. 1994, 59, 4710–4711.
  108. Ishiwata, H.; Sone, H.; Kigoshi, H.; Yamada, K. Total synthesis of doliculide, a potent cytotoxic cyclodepsipeptide from the Japanese sea hare Dolabella auricularia. J. Org. Chem. 1994, 59, 4712–4713.
  109. Matcha, K.; Madduri, A.V.R.; Roy, S.; Ziegler, S.; Waldmann, H.; Hirsch, A.K.H.; Minnaard, A.J. Total synthesis of (-)-doliculide, structure-activity relationship studies and its binding to F-actin. ChemBioChem 2012, 13, 2537–2548.
  110. Foerster, F.; Braig, S.; Chen, T.; Altmann, K.H.; Vollmar, A.M. Pharmacological characterization of actin-binding (-)-doliculide. Bioorganic Med. Chem. 2015, 22, 5117–5122.
  111. Kimura, J.; Takada, Y.; Inayoshi, T.; Nakao, Y.; Goetz, G.; Yoshida, W.Y.; Scheuer, P.J. Kulokekahilide-1, a cytotoxic depsipeptide from the cephalaspidean mollusk Philinopsis speciosa. J. Org. Chem. 2002, 67, 1760–1767.
  112. Nakao, Y.; Yoshida, W.Y.; Takada, Y.; Kimura, J.; Yang, L.; Mooberry, S.L.; Scheuer, P.J. Kulokekahilide-2, a cytotoxic depsipeptide from a cephalaspidean mollusk Philinopsis speciosa. J. Nat. Prod. 2004, 67, 1332–1340.
  113. Umehara, M.; Negishi, T.; Tashiro, T.; Nakao, Y.; Kimura, J. Structure-related cytotoxic activity of derivatives from kulokekahilide-2, a cyclodepsipeptide in Hawaiian marine mollusk. Bioorganic Med. Chem. Lett. 2012, 22, 7422–7425.
  114. Umehara, M.; Negishi, T.; Maehara, Y.; Nakao, Y.; Kimura, J. Stereochemical analysis and cytotoxicity of kulokekahilide-2 and its analogues. Tetrahedron 2013, 69, 3045–3053.
  115. Von Schwarzenberg, K.; Vollmar, A.M. Targeting apoptosis pathways by natural compounds in cancer: Marine compounds as lead structures and chemical tools for cancer therapy. Cancer Lett. 2013, 332, 295–303.
  116. Martín-Algarra, S.; Espinosa, E.; Rubió, J.; López, J.J.L.; Manzano, J.L.; Carrión, L.A.; Plazaola, A.; Tanovic, A.; Paz-Ares, L. Phase II study of weekly kahalalide F in patients with advanced malignant melanoma. Eur. J. Cancer 2009, 45, 732–735.
  117. Gao, J.; Hamann, M.T. Chemistry and biology of lipids. Chem. Rev. 2009, 53, 35–43.
  118. El Gamal, A.A. Biological importance of marine algae. Saudi Pharm. J. 2010, 18, 1–25.
  119. Xu, W.J.; Liao, X.J.; Xu, S.H.; Diao, J.Z.; Du, B.; Zhou, X.L.; Pan, S.S. Isolation, structure determination, and synthesis of galaxamide, a rare cytotoxic cyclic pentapeptide from a marine algae Galaxaura filamentosa. Org. Lett. 2008, 10, 4569–4572.
  120. Lunagariya, J.; Liao, X.; Long, W.; Zhong, S.; Bhadja, P.; Li, H.; Zhao, B.; Xu, S. Cytotoxicity study of cyclopentapeptide analogues of marine natural product galaxamide towards human breast cancer cells. Oxid. Med. Cell. Longev. 2017, 2017.
  121. Allkin, B. Useful Plants–Medicines: At Least 28,187 Plant Species are Currently Recorded as Being of Medicinal Use. In State of the World’s Plants 201; Royal Botanic Gardens, Kew: London, UK, 2017.
  122. Wu, D.; Gao, Y.; Qi, Y.; Chen, L.; Ma, Y.; Li, Y. Peptide-based cancer therapy: Opportunity and challenge. Cancer Lett. 2014, 351, 13–22.
  123. Wélé, A.; Zhang, Y.; Ndoye, I.; Brouard, J.P.; Pousset, J.L.; Bodo, B. A cytotoxic cyclic heptapeptide from the seeds of Annona cherimola. J. Nat. Prod. 2004, 67, 1577–1579.
  124. Wélé, A.; Ndoye, I.; Zhang, Y.; Brouard, J.P.; Bodo, B. Cherimolacyclopeptide D, a novel cycloheptapeptide from the seeds of Annona cherimola. Phytochemistry 2005, 66, 693–696.
  125. Wélé, A.; Zhang, Y.; Brouard, J.P.; Pousset, J.L.; Bodo, B. Two cyclopeptides from the seeds of Annona cherimola. Phytochemistry 2005, 66, 2376–2380.
  126. Idrissa, N.; Adama, D.; Mamadou, B.; Rokhaya, S.G.; Yoro, T. Novel cytotoxic cycloheptapeptide from the latex of Jatropha integerrima. J. Chem. Pharm. Res. 2016, 8, 135–139.
  127. Mongkolvisut, W.; Sutthivaiyakit, S.; Leutbecher, H.; Mika, S.; Klaiber, I.; Möller, W.; Rösner, H.; Beifuss, U.; Conrad, J. Integerrimides A and B, cyclic heptapeptides from the latex of Jatropha integerrima. J. Nat. Prod. 2006, 69, 1435–1441.
  128. Goyal, A.; Sharma, V.; Upadhyay, N.; Gill, S.; Sihag, M. Flax and flaxseed oil: An ancient medicine & modern functional food. J. Food Sci. Technol. 2014, 51, 1633–1653.
  129. Okinyo-Owiti, D.P.; Dong, Q.; Ling, B.; Jadhav, P.D.; Bauer, R.; Maley, J.M.; Reaney, M.J.T.; Yang, J.; Sammynaiken, R. Evaluating the cytotoxicity of flaxseed orbitides for potential cancer treatment. Toxicol. Rep. 2015, 2, 1014–1018.
  130. Lomchoey, N.; Panseeta, P.; Boonsri, P.; Apiratikul, N.; Prabpai, S.; Kongsaeree, P.; Suksamrarn, S. New bioactive cyclopeptide alkaloids with rare terminal unit from the root bark of: Ziziphus cambodiana. RSC Adv. 2018, 8, 18204–18215.
  131. Hsieh, P.-W.; Chang, F.-R.; Wu, C.-C.; Li, C.-M.; Wu, K.-Y.; Chen, S.-L.; Yen, H.-F.; Wu, Y.-C. Longicalycinin A, a New cytotoxic cyclic peptide from Dianthus superbus var. longicalycinus (MAXIM.) WILL. Chem. Pharm. Bull. 2005, 53, 336–338.
  132. Ahmad, W. Solid-phase total synthesis of cyclic pentapeptide longicalycinin A, by using 2-chlorotrityl chloride resin. J. Cancer Res. Exp. Oncol. 2014, 5, 8–19.
  133. HoushdarTehrani, M.H.; Bamoniri, A.; Mirjalili, B.B.F.; Gholibeikian, M. Synthesis of linear and cyclic disulfide heptapeptides of longicalycinin a and evaluation of toxicity on cancerous cells HepG2 and HT-29. Iran. J. Pharm. Res. 2018, 17, 956–963.
  134. Hsieh, P.W.; Chang, F.R.; Wu, C.C.; Wu, K.Y.; Li, C.M.; Chen, S.L.; Wu, Y.C. New cytotoxic cyclic peptides and dianthramide from Dianthus superbus. J. Nat. Prod. 2004, 67, 1522–1527.
  135. Shim, Y.Y.; Young, L.W.; Arnison, P.G.; Gilding, E.; Reaney, M.J.T. Proposed systematic nomenclature for orbitides. J. Nat. Prod. 2015, 78, 645–652.
  136. Beirigo, P.J.S.D.; Torquato, H.F.V.; Santos, C.H.C.D.; de Carvalho, M.G.; Castro, R.N.; Paredes-Gamero, E.J.; de Sousa, P.T.; Jacinto, M.J.; da Silva, V.C. [1-8-NαlC]-Zanriorb A1, a proapoptotic orbitide from leaves of Zanthoxylum riedelianum. J. Nat. Prod. 2016, 79, 1454–1458.
  137. Lv, J.P.; Yang, S.; Dong, J.X.; Jin, H. New cyclopeptide alkaloids from the whole plant of Justicia procumbens L. Nat. Prod. Res. 2020, 1–9.
  138. Liu, Z.; Fu, J.; Xiao, S.; Wang, D. Structural characterization of ginseng cyclopeptides and detection of capability to induce apoptosis in gastrointestinal cancer cells. RSC Adv. 2019, 9, 29847–29855.
  139. Craik, D.J.; Daly, N.L.; Bond, T.; Waine, C. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. J. Mol. Biol. 1999, 294, 1327–1336.
  140. Craik, D.J.; Cemazar, M.; Wang, C.K.L.; Daly, N.L. The cyclotide family of circular miniproteins: Nature’s combinatorial peptide teplate. Biopolymer 2006, 84, 250–266.
  141. Zhao, S.M.; Kuang, B.; Fan, J.T.; Yan, H.; Xu, W.Y.; Tan, N.H. Antitumor cyclic hexapeptides from Rubia plants: History, chemistry, and mechanism (2005–2011). Chim. Int. J. Chem. 2011, 65, 952–956.
  142. Figueiredo, P.O.; Matos, M.D.F.C.; Perdomo, R.T.; Kato, W.H.; Barros, M.V.G.O.; Garcez, F.R.; Garcez, W.S. Rubiaceae-type cyclopeptides from Galianthe thalictroides. J. Nat. Prod. 2016, 79, 1165–1169.
  143. Wang, Z.; Zhao, S.M.; Zhao, L.M.; Chen, X.Q.; Zeng, G.Z.; Tan, N.H. Rubipodanin A, the first natural ndesmonomethyl rubiaceae-type cyclopeptide from rubia podantha, indicating an important role of the n9- methyl group in the conformation and bioactivity. PLoS ONE 2015, 10, e0144950.
  144. Hu, Y.Y.; Feng, L.; Wang, J.; Zhang, X.J.; Wang, Z.; Tan, N.H. Rubipodanin B, a new cytotoxic cyclopeptide from Rubia podantha. Chem. Biodivers. 2019, 16, 16–21.
  145. Wang, Y.; Guo, D.; He, J.; Song, L.; Chen, H.; Zhang, Z.; Tan, N. Inhibition of fatty acid synthesis arrests colorectal neoplasm growth and metastasis: Anti-cancer therapeutical effects of natural cyclopeptide RA-XII. Biochem. Biophys. Res. Commun. 2019, 512, 819–824.
  146. Leung, H.W.; Zhao, S.M.; Yue, G.G.L.; Lee, J.K.M.; Fung, K.P.; Leung, P.C.; Tan, N.H.; Lau, C.B.S. RA-XII inhibits tumour growth and metastasis in breast tumour-bearing mice via reducing cell adhesion and invasion and promoting matrix degradation. Sci. Rep. 2015, 5, 1–17.
  147. Song, L.; Wang, Z.; Wang, Y.; Guo, D.; Yang, J.; Chen, L.; Tan, N. Natural cyclopeptide RA-XII, a new autophagy inhibitor, suppresses protective autophagy for enhancing apoptosis through AMPK/mTOR/P70S6K pathways in HepG2 Cells. Molecules 2017, 22, 1934.
  148. Wang, J.; Wang, J.; Li, L.; Feng, L.; Wang, Y.R.; Wang, Z.; Tan, N.H. RA-XII, a bicyclic hexapeptidic glucoside isolated from Rubia yunnanensis Diels, exerts antitumor activity by inhibiting protective autophagy and activating Akt-mTOR pathway in colorectal cancer cells. J. Ethnopharmacol. 2021, 266, 113438.
  149. Hitotsuyanagi, Y.; Hirai, M.; Odagiri, M.; Komine, M.; Hasuda, T.; Fukaya, H.; Takeya, K. RA-XXV and RA-XXVI, Bicyclic hexapeptides from Rubia cordifolia L.: Structure, synthesis, and conformation. Chem. Asian J. 2019, 14, 205–215.
  150. Ding, X.; Bai, D.; Qian, J. Novel cyclotides from Hedyotis biflora inhibit proliferation and migration of pancreatic cancer cell in vitro and in vivo. Med. Chem. Res. 2014, 23, 1406–1413.
  151. Nguyen, G.K.T.; Zhang, S.; Nguyen, N.T.K.; Nguyen, P.Q.T.; Chiu, M.S.; Hardjojo, A.; Tam, J.P. Discovery and characterization of novel cyclotides originated from chimeric precursors consisting of albumin-1 chain a and cyclotide domains in the Fabaceae family. J. Biol. Chem. 2011, 286, 24275–24287.
  152. Zhang, S.; Xiao, K.Z.; Jin, J.; Zhang, Y.; Zhou, W. Chemosensitizing activities of cyclotides from clitoria ternatea in paclitaxel-resistant lung cancer cells. Oncol. Lett. 2013, 5, 641–644.
  153. Gerlach, U.; Burman, S.L.; Debasis Monda, R.; Goransson, D. Characterization and bioactivity of cyclotides from Psychotria leptothyrsa (Rubiaceae). J. Nat. Prod. 2010, 73, 1207–1213.
  154. Hashempour, H.; Koehbach, J.; Daly, N.L.; Ghassempour, A.; Gruber, C.W. Characterizing circular peptides in mixtures: Sequence fragment assembly of cyclotides from a violet plant by MALDI-TOF/TOF mass spectrometry. Amino Acids. 2013, 44, 581–595.
  155. Esmaeili, M.A.; Abagheri-Mahabadi, N.; Hashempour, H.; Farhadpour, M.; Gruber, C.W.; Ghassempour, A. Viola plant cyclotide vigno 5 induces mitochondria-mediated apoptosis via cytochrome C release and caspases activation in cervical cancer cells. Fitoterapia 2016, 109, 162–168.
  156. Herrmann, A.; Svangård, E.; Claeson, P.; Gullbo, J.; Bohlin, L.; Göransson, U. Key role of glutamic acid for the cytotoxic activity of the cyclotide cycloviolacin O2. Cell. Mol. Life Sci. 2006, 63, 235–245.
  157. Burman, R.; Svedlund, E.; Felth, J.; Hassan, S.; Herrmann, A.; Clark, R.J.; Craik, D.J.; Bohlin, L.; Claeson, P.; Göransson, U.; et al. Evaluation of toxicity and antitumor activity of cycloviolacin O2 in mice. Biopolymers 2010, 94, 626–634.
  158. Svangård, E.; Burman, R.; Gunasekera, S.; Lövborg, H.; Gullbo, J.; Göransson, U. Mechanism of action of cytotoxic cyclotides: Cycloviolacin O2 disrupts lipid membranes. J. Nat. Prod. 2007, 70, 643–647.
  159. Gerlach, S.L.; Rathinakumar, R.; Chakravarty, G.; Göransson, U.; Wimley, W.C.; Darwin, S.P.; Mondal, D. Anticancer and chemosensitizing abilities of cycloviolacin 02 from Viola odorata and psyle cyclotides from Psychotria leptothyrsa. Biopolymers 2010, 94, 617–625.
  160. Gerlach, S.L.; Yeshak, M.; Göransson, U.; Roy, U.; Izadpanah, R.; Mondal, D. Cycloviolacin O2 (CyO2) suppresses productive infection and augments the antiviral efficacy of nelfinavir in HIV-1 infected monocytic cells. Biopolymers 2013, 100, 471–479.
  161. He, W.; Yue, L.; Zeng, G.; Daly, N.L.; Craik, D.J.; Tan, N. Peptides Isolation and characterization of cytotoxic cyclotides from Viola philippica. Peptides 2011, 32, 1719–1723.
  162. Yeshak, M.Y.; Burman, R.; Asres, K.; Göransson, U. Cyclotides from an extreme habitat: Characterization of cyclic peptides from Viola abyssinica of the Ethiopian highlands. J. Nat. Prod. 2011, 74, 727–731.
  163. Herrmann, A.; Burman, R.; Mylne, J.S.; Karlsson, G.; Gullbo, J.; Craik, D.J.; Clark, R.J.; Göransson, U. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. Phytochemistry 2008, 69, 939–952.
  164. Svangård, E.; Göransson, U.; Hocaoglu, Z.; Gullbo, J.; Larsson, R.; Claeson, P.; Bohlin, L. Cytotoxic cyclotides from Viola tricolor. J. Nat. Prod. 2004, 67, 144–147.
  165. Jun, T.; Wang, C.K.; Pan, X.; Yan, H.; Zeng, G.; Xu, W.; He, W.; Chan, L.Y.; Zeng, G.; Daly, N.L.; et al. Isolation and characterization of cytotoxic cyclotides from Viola tricolor. Peptides 2010, 32, 1719–1723.
More
Video Production Service