Table of Contents Author Guidelines Submit a Manuscript
Evidence-Based Complementary and Alternative Medicine
Volume 2014, Article ID 904958, 21 pages
http://dx.doi.org/10.1155/2014/904958
Review Article

Recent Advances in Developing Insect Natural Products as Potential Modern Day Medicines

1Laboratório de Biologia de Insetos, Departamento de Biologia Geral, Universidade Federal Fluminense, Niterói, RJ, Brazil
2Department of Biosciences, College of Science, Swansea University, Singleton Park, Swansea SA2 8PP, UK
3Laboratório de Bioquímica e Fisiologia de Insetos, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz, Avenida Brasil 4365, 21045-900 Rio de Janeiro, RJ, Brazil

Received 1 December 2013; Accepted 28 January 2014; Published 6 May 2014

Academic Editor: Ronald Sherman

Copyright © 2014 Norman Ratcliffe et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. E. P. Cherniack, “Bugs as drugs, part 1: insects. The “new” alternative medicine for the 21st century?” Alternative Medicine Review, vol. 15, no. 2, pp. 124–135, 2010. View at Google Scholar · View at Scopus
  2. A. T. Dossey, “Insects and their chemical weaponry: new potential for drug discovery,” Natural Product Reports, vol. 27, no. 12, pp. 1737–1757, 2010. View at Publisher · View at Google Scholar · View at Scopus
  3. N. A. Ratcliffe, C. B. Mello, E. S. Garcia, T. M. Butt, and P. Azambuja, “Insect natural products and processes: new treatments for human disease,” Insect Biochemistry and Molecular Biology, vol. 41, no. 10, pp. 747–769, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. F. Zhu, X. H. Ma, and C. Qin, “Drug discovery prospect from untapped species: indications from approved natural product drugs,” PLoS ONE, vol. 7, no. 7, Article ID e39782, 2012. View at Publisher · View at Google Scholar
  5. P. W. Taylor, “Alternative natural sources for a new generation of antibacterial agents,” International Journal of Antimicrobial Agents, vol. 42, pp. 195–201, 2013. View at Google Scholar
  6. H. Zhao, X. Feng, W. Han et al., “Enhanced binding to and killing of hepatocellular carcinoma cells in vitro by melittin when linked with a novel targeting peptide screened from phage display,” Journal of Peptide Science, vol. 19, pp. 639–650, 2013. View at Google Scholar
  7. M. Kuczer, A. Majewska, and R. Zahorska, “New alloferon analogues: synthesis and antiviral properties,” Chemical Biology and Drug Design, vol. 81, pp. 302–309, 2013. View at Google Scholar
  8. C. Y. Koh, S. Kumar, M. Kazimirova et al., “Crystal structure of thrombin in complex with s-variegin: insights of a novel mechanism of inhibition and design of tunable thrombin inhibitors,” PLoS ONE, vol. 6, no. 10, Article ID e26367, 2011. View at Publisher · View at Google Scholar · View at Scopus
  9. R. W. Pemberton, “Insects and other arthropods used as drugs in Korean traditional medicine,” Journal of Ethnopharmacology, vol. 65, no. 3, pp. 207–216, 1999. View at Publisher · View at Google Scholar · View at Scopus
  10. A. Gomes, M. A. Alam, S. Bhattacharya et al., “Ethno biological usage of zoo products in rheumatoid arthritis,” Indian Journal of Experimental Biology, vol. 49, no. 8, pp. 565–573, 2011. View at Google Scholar · View at Scopus
  11. G. J. Lockhart, “Ants and other great medicines,” partially published online by A. L. Jacobson, 2007, http://www.arthurleej.com/ants.pdf.
  12. R. Dunn, “Insects as medicines: the ant and the grasshopper,” http://www.robrdunn.com/.
  13. S. K. Srivastava, N. Babau, and H. Pandey, “Traditional insect bioprospecting-as human food and medicine,” Indian Journal of Traditional Knowledge, vol. 8, no. 4, pp. 485–494, 2009. View at Google Scholar
  14. E. M. Costa-Neto, “The use of insects in folk medicine in the state of Bahia, northeastern Brazil, with notes on insects reported elsewherein Brazilian folk medicine,” Human Ecology, vol. 30, no. 2, pp. 245–263, 2002. View at Publisher · View at Google Scholar · View at Scopus
  15. D. S. Lee, S. Sinno, and A. Khachemoune, “Honey and wound healing: an overview,” The American Journal of Clinical Dermatology, vol. 12, no. 3, pp. 181–190, 2011. View at Publisher · View at Google Scholar · View at Scopus
  16. N. S. Al-Waili, K. Salom, and A. A. Al-Ghamdi, “Honey for wound healing, ulcers, and burns; data supporting its use in clinical practice,” TheScientificWorldJournal, vol. 11, pp. 766–787, 2011. View at Publisher · View at Google Scholar · View at Scopus
  17. A. Seckam and R. Cooper, “Understanding how honey impacts on wounds: an update on recent research findings,” Wounds International, vol. 4, no. 1, pp. 20–24, 2013. View at Google Scholar
  18. A. B. Jull, A. Rodgers, and N. Walker, “Honey as a topical treatment for wounds,” Cochrane Database of Systematic Reviews, no. 4, Article ID CD005083, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. F. E. Brölmann, D. T. Ubbink, E. A. Nelson et al., “Evidence based decisions for local and systemic wound care,” British Journal of Surgery, vol. 99, no. 9, pp. 1172–1183, 2012. View at Google Scholar
  20. M. B. Abubakar, W. Z. Abdullah, S. A. Sulaiman, and A. B. Suen, “A review of molecular mechanisms of the anti-leukemic effects of phenolic compounds in honey,” International Journal of Molecular Sciences, vol. 13, pp. 15054–15073, 2012. View at Google Scholar
  21. A. J. Tonks, E. Dudley, N. G. Porter et al., “A 5.8-kDa component of manuka honey stimulates immune cells via TLR4,” Journal of Leukocyte Biology, vol. 82, no. 5, pp. 1147–1155, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. P. H. S. Kwakman, A. A. te Velde, L. de Boer, C. M. J. E. Vandenbroucke-Grauls, and S. A. J. Zaat, “Two major medicinal honeys have different mechanisms of bactericidal activity,” PLoS ONE, vol. 6, no. 3, Article ID e17709, 2011. View at Publisher · View at Google Scholar · View at Scopus
  23. S. Alnaimat, M. Wainwright, and K. Al’Abri, “Antibacterial potential of honey from different origins: a comparison with Manuka honey,” Journal of Microbiology, Biotechnology and Food Sciences, vol. 1, no. 5, pp. 1328–1338, 2012. View at Google Scholar
  24. R. E. Jenkins and R. Cooper, “Synergy between oxacillin and manuka honey sensitizes methicillin-resistant Staphylococcus aureus to oxacillin,” Journal Antimicrobial Chemotherapy, vol. 67, no. 6, pp. 1405–1407, 2012. View at Publisher · View at Google Scholar
  25. R. A. Cooper, E. Lindsay, and P. C. Molan, “Testing the susceptibility to manuka honey of streptococci isolated from wound swabs,” Journal of ApiProduct & ApiMedical Science, vol. 3, no. 3, pp. 117–122, 2011. View at Google Scholar
  26. A. F. Henriques, R. E. Jenkins, N. F. Burton, and R. A. Cooper, “The effect of manuka honey on the structure of Pseudomonas aeruginosa,” European Journal of Clinical Microbiology and Infectious Diseases, vol. 30, no. 2, pp. 167–171, 2011. View at Publisher · View at Google Scholar · View at Scopus
  27. A. E. Roberts, S. E. Maddocks, and R. A. Cooper, “Manuka honey is bactericidal against Pseudomonas aeruginosa and results in differential expression of OprF and algD,” Microbiology, vol. 158, no. 12, pp. 3005–3013, 2012. View at Google Scholar
  28. K. Brudzynski, K. Abubaker, and T. Wang, “Powerful killing by buckwheat honeys is concentration-dependent, involves complete DNA degradation and requires hydrogen peroxide,” Frontiers in Microbiology, vol. 3, article 242, 2012. View at Publisher · View at Google Scholar
  29. S. E. Maddocks, M. S. Lopez, R. S. Rowlands, and R. A. Cooper, “Manuka honey inhibits the development of Streptococcus pyogenes biofilms and causes reduced expression of two fibronectin binding proteins,” Microbiology, vol. 158, no. 3, pp. 781–790, 2012. View at Publisher · View at Google Scholar · View at Scopus
  30. L. Boukraâa and S. A. Sulaiman, “Rediscovering the antibiotics of the hive,” Recent Patents on Anti-Infective Drug Discovery, vol. 4, no. 3, pp. 206–213, 2009. View at Publisher · View at Google Scholar · View at Scopus
  31. J. M. Sforcin and V. Bankova, “Propolis: is there a potential for the development of new drugs?” Journal of Ethnopharmacology, vol. 133, no. 2, pp. 253–260, 2011. View at Publisher · View at Google Scholar · View at Scopus
  32. N. Oršolić, “Bee honey and cancer,” Journal of ApiProduct and ApiMedical Science, vol. 1, no. 4, pp. 93–103, 2009. View at Google Scholar
  33. C. Spagnuolo, M. Russo, S. Bilotto et al., “Dietary polyphenols in cancer prevention: the example of the flavonoid quercetin in leukemia,” Annals New York Academy of Science, vol. 1259, pp. 95–103, 2012. View at Google Scholar
  34. E. Szliszka and W. Krol, “Polyphenols isolated from propolis augment TRAIL-induced apoptosis in cancer cells,” Evidence-Based Complementary and Alternative Medicine, vol. 2013, Article ID 731940, 10 pages, 2013. View at Publisher · View at Google Scholar
  35. A. Budhraja, N. Gao, Z. Zhang et al., “Apigenin induces apoptosis in human leukemia cells and exhibits anti-leukemic activity in vivo,” Molecular Cancer Therapeutics, vol. 11, no. 1, pp. 132–142, 2012. View at Publisher · View at Google Scholar · View at Scopus
  36. M. J. Fernandez-Cabezudo, R. El-Kharrag, F. Torab et al., “Intravenous administration of manuka honey inhibits tumor growth and improves host survival when used in combination with chemotherapy in a melanoma mouse model,” PLoS ONE, vol. 8, no. 2, Article ID e55993, 2013. View at Publisher · View at Google Scholar
  37. D. R. Hoffman, “Ant venoms,” Current Opinion in Allergy and Clinical Immunology, vol. 10, no. 4, pp. 342–346, 2010. View at Publisher · View at Google Scholar · View at Scopus
  38. E. L. Danneels, D. B. Rivers, and D. C. de Graaf, “Venom proteins of the parasitoid wasp Nasonia vitripennis: recent discovery of an untapped pharmacopee,” Toxins, vol. 2, no. 4, pp. 494–516, 2010. View at Publisher · View at Google Scholar · View at Scopus
  39. J. Matysiak, C. E. H. Schmelzer, R. H. H. Neubert, and Z. J. Kokot, “Characterization of honeybee venom by MALDI-TOF and nanoESI-QqTOF mass spectrometry,” Journal of Pharmaceutical and Biomedical Analysis, vol. 54, no. 2, pp. 273–278, 2011. View at Publisher · View at Google Scholar · View at Scopus
  40. G. Gajski and V. Garaj-Vrhovac, “Melittin: a lytic peptide with anticancer properties,” Environmental Toxicology and Pharmacology, vol. 36, no. 2, pp. 697–705, 2013. View at Google Scholar
  41. T. C. Terwilliger and D. Eisenberg, “The structure of melittin. II. Interpretation of the structure,” Journal of Biological Chemistry, vol. 257, no. 11, pp. 6016–6022, 1982. View at Google Scholar · View at Scopus
  42. N. Oršolić, “Bee venom in cancer therapy,” Cancer Metastasis Reviews, vol. 31, pp. 173–194, 2012. View at Google Scholar
  43. M.-T. Lee, T.-L. Sun, W.-C. Hung et al., “Process of inducing pores in membranes by melittin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 35, pp. 14243–14248, 2013. View at Publisher · View at Google Scholar
  44. S. V. Sharma, “Melittin resistance: a counterselection for ras transformation,” Oncogene, vol. 7, no. 2, pp. 193–201, 1992. View at Google Scholar · View at Scopus
  45. H. G. Zhu, I. Tayeh, L. Israel, and M. Castagna, “Different susceptibility of lung cell lines to inhibitors of tumor promotion and inducers of differentiation,” Journal of Biological Regulators and Homeostatic Agents, vol. 5, no. 2, pp. 52–58, 1991. View at Google Scholar · View at Scopus
  46. Y. H. Zhao, Y. Bai, H. Cui et al., “Design and expression in Pichia pastoris of melittin and research of antibacterial activity increasing of melittin,” Shengming Kexue Yanjiu, vol. 10, no. 4, pp. 313–319, 2006 (Chinese). View at Google Scholar
  47. S. Vuorenoja, A. Rivero-Müller, A. J. Ziecik, I. Huhtaniemi, J. Toppari, and N. A. Rahman, “Targeted therapy for adrenocortical tumors in transgenic mice through their LH receptor by Hecate-human chorionic gonadotropin β conjugate,” Endocrine-Related Cancer, vol. 15, no. 2, pp. 635–648, 2008. View at Publisher · View at Google Scholar · View at Scopus
  48. H. Zhao, X. Feng, W. Han et al., “Enhanced binding to and killing of hepatocellular carcinoma cells in vitro by melittin when linked with a novel targeting peptide screened from phage display,” Journal of Peptide Science, vol. 19, pp. 639–650, 2013. View at Google Scholar
  49. D. Winder, W. H. Günzburg, V. Erfle, and B. Salmons, “Expression of antimicrobial peptides has an antitumour effect in human cells,” Biochemical and Biophysical Research Communications, vol. 242, no. 3, pp. 608–612, 1998. View at Publisher · View at Google Scholar · View at Scopus
  50. N. R. Soman, S. L. Baldwin, G. Hu et al., “Molecularly targeted nanocarriers deliver the cytolytic peptide melittin specifically to tumor cells in mice, reducing tumor growth,” Journal of Clinical Investigation, vol. 119, no. 9, pp. 2830–2842, 2009. View at Publisher · View at Google Scholar · View at Scopus
  51. C. Huang, H. Jin, Y. Qian et al., “Hybrid melittin cytolytic peptide-driven ultrasmall lipid nanoparticles block melanoma growth in vivo,” ACS Nano, vol. 7, no. 7, pp. 5791–5800, 2013. View at Google Scholar
  52. S. Dosler and A. A. Gerceker, “In vitro activities of antimicrobial cationic peptides: melittin and nisin, alone or in combination with antibiotics against Gram-positive bacteria,” Journal of Chemotherapy, vol. 24, no. 3, pp. 137–143, 2012. View at Google Scholar
  53. J. L. Hood, A. P. Jallouk, N. Campbell et al., “Cytolytic nanoparticles attenuate HIV-1 infectivity,” Antiviral Therapy, vol. 18, no. 1, pp. 95–103, 2013. View at Google Scholar
  54. M. Y. Ahn, S. H. Shim, H. K. Jeong, and K. S. Ryu, “Purification of a dimethyladenosine compound from silkworm pupae as a vasorelaxation substance,” Journal of Ethnopharmacology, vol. 117, no. 1, pp. 115–122, 2008. View at Publisher · View at Google Scholar · View at Scopus
  55. T. D. Sutherland, J. H. Young, S. Weisman, C. Y. Hayashi, and D. J. Merritt, “Insect silk: one name, many materials,” Annual Review of Entomology, vol. 55, pp. 171–188, 2010. View at Publisher · View at Google Scholar · View at Scopus
  56. M. Widhe, J. Johansson, M. Hedhammar, and A. Rising, “Current progress and limitations of spider silk for biomedical applications,” Biopolymers, vol. 97, no. 6, pp. 468–478, 2012. View at Publisher · View at Google Scholar · View at Scopus
  57. T. D. Sutherland, S. Weisman, A. A. Walker, and S. T. Mudie, “The coiled coil silk of bees, ants, and hornets,” Biopolymers, vol. 97, no. 6, pp. 446–454, 2012. View at Publisher · View at Google Scholar · View at Scopus
  58. K. Numata, B. Subramanian, H. A. Currie, and D. L. Kaplan, “Bioengineered silk protein-based gene delivery systems,” Biomaterials, vol. 30, no. 29, pp. 5775–5784, 2009. View at Publisher · View at Google Scholar · View at Scopus
  59. K. Numata and D. L. Kaplan, “Silk-based delivery systems of bioactive molecules,” Advanced Drug Delivery Reviews, vol. 62, no. 15, pp. 1497–1508, 2010. View at Publisher · View at Google Scholar · View at Scopus
  60. A. C. MacIntosh, V. R. Kearns, A. Crawford, and P. V. Hatton, “Skeletal tissue engineering using silk biomaterials,” Journal of Tissue Engineering and Regenerative Medicine, vol. 2, no. 2-3, pp. 71–80, 2008. View at Publisher · View at Google Scholar · View at Scopus
  61. The International Silkworm Genome Consortium, “The genome of a lepidopteran model insect, the silkworm Bombyx mori,” Insect Biochemistry and Molecular Biology, vol. 38, no. 12, pp. 1036–1045, 2008. View at Publisher · View at Google Scholar · View at Scopus
  62. S. K. Nitta and K. Numata, “Biopolymer-based nanoparticles for drug/gene delivery and tissue engineering,” International Journal of Molecular Sciences, vol. 14, pp. 1629–1654, 2013. View at Google Scholar
  63. M. Xu and R. V. Lewis, “Structure of a protein superfiber: spider dragline silk,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 18, pp. 7120–7124, 1990. View at Google Scholar · View at Scopus
  64. F. Teulé, Y.-G. Miao, B.-H. Sohn et al., “Silkworms transformed with chimeric silkworm/spider silk genes spin composite silk fibers with improved mechanical properties,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 3, pp. 923–928, 2012. View at Publisher · View at Google Scholar · View at Scopus
  65. K. Numata, J. Hamasaki, B. Subramanian, and D. L. Kaplan, “Gene delivery mediated by recombinant silk proteins containing cationic and cell binding motifs,” Journal of Controlled Release, vol. 146, no. 1, pp. 136–143, 2010. View at Publisher · View at Google Scholar · View at Scopus
  66. K. Numata, M. R. Reagan, R. H. Goldstein, M. Rosenblatt, and D. L. Kaplan, “Spider silk-based gene carriers for tumor cell-specific delivery,” Bioconjugate Chemistry, vol. 22, no. 8, pp. 1605–1610, 2011. View at Publisher · View at Google Scholar · View at Scopus
  67. K. Numata, A. J. Mieszawska-Czajkowska, L. A. Kvenvold, and D. L. Kaplan, “Silk-based nanocomplexes with tumor-homing peptides for tumor-specific gene delivery,” Macromolecular Bioscience, vol. 12, no. 1, pp. 75–82, 2012. View at Publisher · View at Google Scholar · View at Scopus
  68. Q. Zhang, S. Q. Yan, and M. Z. Li, “Porous materials based on Bombyx mori silk fibroin,” Journal of Fiber Bioengineering and Informatics, vol. 3, no. 1, pp. 1–8, 2010. View at Publisher · View at Google Scholar
  69. F. P. Seib, M. Herklotz, K. A. Burke et al., “Multifunctional silk-heparin biomaterials for vascular tissue engineering applications,” Biomaterials, vol. 35, no. 1, pp. 83–91, 2014. View at Google Scholar
  70. F. P. Seib, E. M. Pritchard, and D. L. Kaplan, “Self-assembling doxorubicin silk hydrogels for the focal treatment of primary breast cancer,” Advanced Functional Materials, vol. 23, no. 1, pp. 58–65, 2013. View at Google Scholar
  71. E. M. Pritchard, T. Valentin, B. Panilaitis et al., “Antibiotic-releasing silk biomaterials for infection prevention and treatment,” Advanced Functional Materials, vol. 23, no. 7, pp. 854–861, 2012. View at Google Scholar
  72. M. Hronik-Tupaj, W. K. Raja, M. Tang-Schomer, F. G. Omenetto, and D. L. Kaplan, “Neural responses to electrical stimulation on patterned silk films,” Journal of Biomedical Materials Research A, vol. 101, no. 9, pp. 2559–2572, 2013. View at Google Scholar
  73. J. Zhang, E. Pritchard, X. Hu et al., “Stabilization of vaccines and antibiotics in silk and eliminating the cold chain,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 30, pp. 11981–11986, 2013. View at Publisher · View at Google Scholar
  74. X. Sheng, L. Fan, C. He et al., “Vitamin E-loaded silk fibroin nanofibrous mats fabricated by green process for skin care application,” International Journal of Biological Macromolecules, vol. 56, pp. 49–56, 2013. View at Google Scholar
  75. O. Tokareva, V. A. Michalczechen-Lacerda, E. L. Rech et al., “Recombinant DNA production of spider silk proteins,” Microbial Biotechnology, vol. 6, no. 6, pp. 651–663, 2013. View at Google Scholar
  76. R. Rajkhowa, T. Tsuzuki, and X. G. Wang, “Recent innovations in silk biomaterials,” Journal of Fiber Bioengineering and Informatics, vol. 2, no. 4, pp. 202–213, 2010. View at Google Scholar
  77. M. A. Bologna and J. D. Pinto, “Phylogenetic studies of Meloidae (Coleoptera), with emphasis on the evolution of phoresy,” Systematic Entomology, vol. 26, no. 1, pp. 33–72, 2001. View at Publisher · View at Google Scholar · View at Scopus
  78. C. E. P. Galvis, L. Y. V. Mendez, and V. V. Kouznetsov, “Cantharidin-based small molecules as potential therapeutic agents,” Chemical Biology and Drug Design, vol. 82, pp. 477–499, 2013. View at Google Scholar
  79. E. Lissina, B. Young, M. L. Urbanus et al., “A systems biology approach reveals the role of a novel methyltransferase in response to chemical stress and lipid homeostasis,” PLoS Genetics, vol. 7, no. 10, Article ID e1002332, 2011. View at Publisher · View at Google Scholar · View at Scopus
  80. J. Bajsa, A. McCluskey, C. P. Gordon et al., “The antiplasmodial activity of norcantharidin analogs,” Bioorganic and Medicinal Chemistry Letters, vol. 20, no. 22, pp. 6688–6695, 2010. View at Publisher · View at Google Scholar · View at Scopus
  81. F. Ghaffarifar, “Leishmania major: in vitro and in vivo anti-leishmanial effect of cantharidin,” Experimental Parasitology, vol. 126, no. 2, pp. 126–129, 2010. View at Publisher · View at Google Scholar · View at Scopus
  82. I. J. Tseng, S. Y. Sheu, P. Y. Li et al., “Synthesis and evaluation of cantharidinimides on human cancer cells,” Journal of Experimental Clinical Medicine, vol. 4, pp. 280–283, 2012. View at Google Scholar
  83. Y.-P. Zhan, X.-E. Huang, and J. Cao, “Clinical study on safety and efficacy of Qinin (cantharidin sodium) injection combined with chemotherapy in treating patients with gastric cancer,” Asian Pacific Journal of Cancer Prevention, vol. 13, no. 9, pp. 4773–4776, 2012. View at Google Scholar
  84. W. Li, L. Xie, Z. Chen et al., “Cantharidin, a potent and selective PP2A inhibitor, induces an oxidative stress-independent growth inhibition of pancreatic cancer cells through G2/M cell-cycle arrest and apoptosis,” Cancer Science, vol. 101, no. 5, pp. 1226–1233, 2010. View at Publisher · View at Google Scholar · View at Scopus
  85. W.-W. Huang, S.-W. Ko, H.-Y. Tsai et al., “Cantharidin induces G2/M phase arrest and apoptosis in human colorectal cancer colo 205 cells through inhibition of CDK1 activity and caspase-dependent signaling pathways,” International Journal of Oncology, vol. 38, no. 4, pp. 1067–1073, 2011. View at Publisher · View at Google Scholar · View at Scopus
  86. Y.-P. Huang, C.-H. Ni, C.-C. Lu et al., “Suppressions of migration and invasion by cantharidin in TSGH-8301 human bladder carcinoma cells through the inhibitions of matrix metalloproteinase-2/-9 signaling,” Evidence-Based Complementary and Alternative Medicine, vol. 2013, Article ID 190281, 8 pages, 2013. View at Publisher · View at Google Scholar
  87. L. M. Shou, Q. Y. Zhang, W. Li et al., “Cantharidin and norcantharidin inhibit the ability of MCF-7 cells to adhere to platelets via protein kinase C pathway-dependent downregulation of α2 integrin,” Oncology Reports, vol. 30, pp. 1059–1066, 2013. View at Google Scholar
  88. W. Li, D. M. Li, and K. Chen, “Development of a gene therapy strategy to target hepatocellular carcinoma based inhibition of protein phosphatase 2A using the α-fetoprotein promoter enhancer and pgk promoter: an in vitro and in vivo study,” BMC Cancer, vol. 12, article 547, 2012. View at Publisher · View at Google Scholar
  89. Y.-J. Dang and C.-Y. Zhu, “Oral bioavailability of cantharidin-loaded solid lipid nanoparticles,” BMC Chinese Medicine, vol. 8, article 1, 2013. View at Publisher · View at Google Scholar
  90. M. D. Lavine and M. R. Strand, “Insect hemocytes and their role in immunity,” Insect Biochemistry and Molecular Biology, vol. 32, no. 10, pp. 1295–1309, 2002. View at Publisher · View at Google Scholar · View at Scopus
  91. G. Wang, Ed., Antimicrobial Peptides, Advances in Molecular and Cellular Biology Series, CABI, 2010, http://ebookee.org/Antimicrobial-Peptides-Advances-in-Molecular-and-Cellular-Biology-Series-_912403.html.
  92. J. B. Peravali, S. R. Kotra, K. Sobha et al., “Antimicrobial peptides: an effective alternative for antibiotic therapy,” Mintage Journal of Pharmaceutical & Medical Sciences, vol. 2, no. 2, pp. 1–7, 2013. View at Google Scholar
  93. S. J. Kang, D. H. Kim, T. Mishig-Ochir et al., “Antimicrobial peptides: their physicochemical properties and therapeutic application,” Archives of Pharmal Research, vol. 35, no. 3, pp. 409–413, 2012. View at Google Scholar
  94. M. Ntwasa, A. Goto, and S. Kurata, “Coleopteran antimicrobial peptides: prospects for clinical applications,” International Journal of Microbiology, vol. 2012, Article ID 101989, 8 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  95. G. Laverty, S. P. Gorman, and B. F. Gilmore, “The potential of antimicrobial peptides as biocides,” International Journal of Molecular Sciences, vol. 12, no. 10, pp. 6566–6596, 2011. View at Publisher · View at Google Scholar · View at Scopus
  96. E. Guaní-Guerra, T. Santos-Mendoza, S. O. Lugo-Reyes, and L. M. Terán, “Antimicrobial peptides: general overview and clinical implications in human health and disease,” Clinical Immunology, vol. 135, no. 1, pp. 1–11, 2010. View at Publisher · View at Google Scholar · View at Scopus
  97. X. Zhao, H. Wu, and H. Lu, “LAMP: a database linking antimicrobial peptides,” PLoS ONE, vol. 8, no. 6, Article ID e66557, 2013. View at Publisher · View at Google Scholar
  98. N. K. Brogden and K. A. Brogden, “Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals?” International Journal of Antimicrobial Agents, vol. 38, no. 3, pp. 217–225, 2011. View at Publisher · View at Google Scholar · View at Scopus
  99. M. Ntwasa, “Cationic peptide interactions with biological macromolecules,” in Binding Protein, K. Abdelmohsen, Ed., pp. 139–164, InTech Open Access Publishing, 2012. View at Publisher · View at Google Scholar
  100. D. Gaspar, A. S. Veiga, and M. A. R. B. Castanho, “From antimicrobial to anticancer peptides. A review,” Frontiers in Microbiology, vol. 4, article 294, 2013. View at Publisher · View at Google Scholar
  101. D. W. Hoskin and A. Ramamoorthy, “Studies on anticancer activities of antimicrobial peptides,” Biochimica et Biophysica Acta—Biomembranes, vol. 1778, no. 2, pp. 357–375, 2008. View at Publisher · View at Google Scholar · View at Scopus
  102. V. Kokoza, A. Ahmed, S. W. Shin, N. Okafor, Z. Zou, and A. S. Raikhel, “Blocking of Plasmodium transmission by cooperative action of cecropin A and defensin A in transgenic Aedes aegypti mosquitoes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 18, pp. 8111–8116, 2010. View at Publisher · View at Google Scholar · View at Scopus
  103. M. Torrent, D. Pulido, and L. Rivas, “Antimicrobial peptide action on parasites,” Current Drug Targets, vol. 13, pp. 1138–1147, 2012. View at Google Scholar
  104. E. Ostorhazi, M. C. Holub, F. Rozgonyi et al., “Broad-spectrum antimicrobial efficacy of peptide A3-APO in mouse models of multidrug-resistant wound and lung infections cannot be explained by in vitro activity against the pathogens involved,” International Journal of Antimicrobial Agents, vol. 37, no. 5, pp. 480–484, 2011. View at Publisher · View at Google Scholar · View at Scopus
  105. N. Berthold, P. Czihal, S. Fritsche et al., “Novel apidaecin 1b analogs with superior serum stabilities for treatment of infections by gram-negative pathogens,” Antimicrobial Agents and Chemotherapy, vol. 57, no. 1, pp. 402–409, 2013. View at Google Scholar
  106. P. Bulet and R. Stöcklin, “Insect antimicrobial peptides: structures, properties and gene regulation,” Protein and Peptide Letters, vol. 12, no. 1, pp. 3–11, 2005. View at Publisher · View at Google Scholar · View at Scopus
  107. H. Ulm, M. Wilmes, Y. Shai et al., “Antimicrobial host defensins—specific antibiotic activities and innate defense modulation,” Frontiers in Immunology, vol. 3, article 249, 2012. View at Publisher · View at Google Scholar
  108. J. Wiesner and A. Vilcinskas, “Antimicrobial peptides: the ancient arm of the human immune system,” Virulence, vol. 1, no. 5, pp. 440–464, 2010. View at Publisher · View at Google Scholar · View at Scopus
  109. Y. Huang, J. Huang, and Y. Chen, “Alpha-helical cationic antimicrobial peptides: relationships of structure and function,” Protein and Cell, vol. 1, no. 2, pp. 143–152, 2010. View at Publisher · View at Google Scholar · View at Scopus
  110. M. Zaiou, “Multifunctional antimicrobial peptides: therapeutic targets in several human diseases,” Journal of Molecular Medicine, vol. 85, no. 4, pp. 317–329, 2007. View at Publisher · View at Google Scholar · View at Scopus
  111. S. M. Paranjape, T. W. Lauer, R. C. Montelaro et al., “Modulation of proinflammatory activity by the engineered cationic antimicrobial peptide WLBU-2,” F1000Research, vol. 2, article 36, 2013. View at Publisher · View at Google Scholar
  112. D. Ausbacher, G. Svineng, T. Hansen et al., “Anticancer mechanisms of action of two small amphipathic β2, 2-amino acid derivatives derived from antimicrobial peptides,” Biochimica et Biophysica Acta, vol. 1818, pp. 2917–2925, 2012. View at Google Scholar
  113. T. Iwasaki, J. Ishibashi, H. Tanaka et al., “Selective cancer cell cytotoxicity of enantiomeric 9-mer peptides derived from beetle defensins depends on negatively charged phosphatidylserine on the cell surface,” Peptides, vol. 30, no. 4, pp. 660–668, 2009. View at Publisher · View at Google Scholar · View at Scopus
  114. B. Bommarius, H. Jenssen, M. Elliott et al., “Cost-effective expression and purification of antimicrobial and host defense peptides in Escherichia coli,” Peptides, vol. 31, no. 11, pp. 1957–1965, 2010. View at Publisher · View at Google Scholar · View at Scopus
  115. H. Wang, X.-L. Meng, J.-P. Xu, J. Wang, H. Wang, and C.-W. Ma, “Production, purification, and characterization of the cecropin from Plutella xylostella, pxCECA1, using an intein-induced self-cleavable system in Escherichia coli,” Applied Microbiology and Biotechnology, vol. 94, pp. 1031–1039, 2012. View at Publisher · View at Google Scholar · View at Scopus
  116. X. Wang, M. Zhu, G. Yang et al., “Expression of cecropin B in Pichia pastoris and its bioactivity in vitro,” Experimental and Therapeutic Medicine, vol. 2, no. 4, pp. 655–660, 2011. View at Publisher · View at Google Scholar · View at Scopus
  117. J.-J. Huang, J.-C. Lu, and M. Lu, “The design and construction of K11: a novel α-helical antimicrobial peptide,” International Journal of Microbiology, vol. 2012, Article ID 764834, 6 pages, 2012. View at Publisher · View at Google Scholar
  118. S. A. Guralp, Y. E. Murgha, J.-M. Rouillard et al., “From design to screening: a new antimicrobial peptide discovery pipeline,” PLoS ONE, vol. 8, no. 3, Article ID e59305, 2013. View at Publisher · View at Google Scholar
  119. G. Maccari, M. di Luca, R. Nifosi et al., “Antimicrobial peptides design by evolutionary multiobjective optimization,” PLoS Computer Biology, vol. 9, no. 9, Article ID e1003212, 2013. View at Publisher · View at Google Scholar
  120. M. Zasloff, “Antimicrobial peptides of multicellular organisms,” Nature, vol. 415, no. 6870, pp. 389–395, 2002. View at Publisher · View at Google Scholar · View at Scopus
  121. L. F. Fehri, P. Sirand-Pugnet, G. Gourgues, G. Jan, H. Wróblewski, and A. Blanchard, “Resistance to antimicrobial peptides and stress response in Mycoplasma pulmonis,” Antimicrobial Agents and Chemotherapy, vol. 49, no. 10, pp. 4154–4165, 2005. View at Publisher · View at Google Scholar · View at Scopus
  122. A. Giacometti, O. Cirioni, F. Barchiesi, M. Fortuna, and G. Scalise, “In-vitro activity of cationic peptides alone and in combination with clinically used antimicrobial agents against Pseudomonas aeruginosa,” Journal of Antimicrobial Chemotherapy, vol. 44, no. 5, pp. 641–645, 1999. View at Publisher · View at Google Scholar · View at Scopus
  123. G. G. Perron, M. Zasloff, and G. Bell, “Experimental evolution of resistance to an antimicrobial peptide,” Proceedings of the Royal Society B: Biological Sciences, vol. 273, no. 1583, pp. 251–256, 2006. View at Publisher · View at Google Scholar · View at Scopus
  124. S. I. Chernysh and N. A. Gordja, “The immune system of maggots of the blow fly (Calliphora vicina) as a source of medicinal drugs,” Journal of Evolutionary Biochemistry and Physiology, vol. 47, no. 6, pp. 524–533, 2011. View at Publisher · View at Google Scholar · View at Scopus
  125. S.-C. Park, Y. Park, and K.-S. Hahm, “The role of antimicrobial peptides in preventing multidrug-resistant bacterial infections and biofilm formation,” International Journal of Molecular Sciences, vol. 12, no. 9, pp. 5971–5992, 2011. View at Publisher · View at Google Scholar · View at Scopus
  126. M. Kazemzadeh-Narbat, S. Noordin, B. A. Masri et al., “Drug release and bone growth studies of antimicrobial peptide-loaded calcium phosphate coating on titanium,” Journal of Biomedical Materials Research B: Applied Biomaterials, vol. 100, no. 5, pp. 1344–1352, 2012. View at Publisher · View at Google Scholar · View at Scopus
  127. R. A. Sherman, M. J. R. Hall, and S. Thomas, “Medicinal maggots: an ancient remedy for some contemporary afflictions,” Annual Review of Entomology, vol. 45, pp. 55–81, 2000. View at Publisher · View at Google Scholar · View at Scopus
  128. A. Bexfield, A. E. Bond, E. C. Roberts et al., “The antibacterial activity against MRSA strains and other bacteria of a <500 Da fraction from maggot excretions/secretions of Lucilia sericata (Diptera: Calliphoridae),” Microbes and Infection, vol. 10, no. 4, pp. 325–333, 2008. View at Publisher · View at Google Scholar · View at Scopus
  129. R. A. Sherman, “Maggot therapy takes us back to the future of wound care: new and improved maggot therapy for the 21st century,” Journal of Diabetes Science and Technology, vol. 3, no. 2, pp. 336–344, 2009. View at Google Scholar · View at Scopus
  130. A. Vilcinskas, “From traditional maggot therapy to modern biosurgery,” in Insect Biotechnology, A. Vilsinskas, Ed., pp. 67–76, Springer, Dordrecht, The Netherlands, 2010. View at Google Scholar
  131. J. Bohova, J. Majtan, and P. Takac, “Immunomodulatory properties of medicinal maggots Lucilia sericata in wound healing process,” TANG International Journal of Genuine Traditional Medicine, vol. 2, no. 3, pp. 1–7, 2012. View at Google Scholar
  132. L. Chambers, S. Woodrow, A. P. Brown et al., “Degradation of extracellular matrix components by defined proteinases from the greenbottle larva Lucilia sericata used for the clinical debridement of non-healing wounds,” British Journal of Dermatology, vol. 148, no. 1, pp. 14–23, 2003. View at Publisher · View at Google Scholar · View at Scopus
  133. A. Brown, A. Horobin, and D. G. Blount, “Blow fly Lucilia sericata nuclease digests DNA associated with wound slough/eschar and with Pseudomonas aeruginosa biofilm,” Medical and Veterinary Entomology, vol. 26, no. 4, pp. 432–439, 2012. View at Google Scholar
  134. G. Telford, A. P. Brown, A. Rich et al., “Wound debridement potential of glycosidases of the wound-healing maggot, Lucilia sericata,” Medical and Veterinary Entomology, vol. 26, no. 3, pp. 291–299, 2012. View at Google Scholar
  135. A. Bexfield, A. E. Bond, C. Morgan et al., “Amino acid derivatives from Lucilia sericata excretions/secretions may contribute to the beneficial effects of maggot therapy via increased angiogenesis,” British Journal of Dermatology, vol. 162, no. 3, pp. 554–562, 2010. View at Publisher · View at Google Scholar · View at Scopus
  136. Z. Zhang, S. Wang, Y. Diao, J. Zhang, and D. Lv, “Fatty acid extracts from Lucilia sericata larvae promote murine cutaneous wound healing by angiogenic activity,” Lipids in Health and Disease, vol. 9, article 24, 2010. View at Publisher · View at Google Scholar · View at Scopus
  137. M. J. A. van der Plas, A. M. van der Does, M. Baldry et al., “Maggot excretions/secretions inhibit multiple neutrophil pro-inflammatory responses,” Microbes and Infection, vol. 9, no. 4, pp. 507–514, 2007. View at Publisher · View at Google Scholar · View at Scopus
  138. M. J. A. van der Plas, M. Baldry, J. T. van Dissel, G. N. Jukema, and P. H. Nibbering, “Maggot secretions suppress pro-inflammatory responses of human monocytes through elevation of cyclic AMP,” Diabetologia, vol. 52, no. 9, pp. 1962–1970, 2009. View at Publisher · View at Google Scholar · View at Scopus
  139. M. J. A. van der Plas, J. T. van Dissel, and P. H. Nibbering, “Maggot secretions skew monocyte-macrophage differentiation away from a pro-inflammatory to a pro-angiogenic type,” PLoS ONE, vol. 4, no. 11, Article ID e8071, 2009. View at Publisher · View at Google Scholar · View at Scopus
  140. R. A. Elkington, M. Humphries, M. Commins, N. Maugeri, T. Tierney, and T. J. Mahony, “A Lucilia cuprina excretory-secretory protein inhibits the early phase of lymphocyte activation and subsequent proliferation,” Parasite Immunology, vol. 31, no. 12, pp. 750–765, 2009. View at Publisher · View at Google Scholar · View at Scopus
  141. G. Cazander, M. W. J. Schreurs, L. Renwarin et al., “Maggot excretions affect the human complement system,” Wound Repair and Regeneration, vol. 20, pp. 879–886, 2012. View at Google Scholar
  142. V. Čeřovský, J. Žďárek, V. Fučík, L. Monincová, Z. Voburka, and R. Bém, “Lucifensin, the long-sought antimicrobial factor of medicinal maggots of the blowfly Lucilia sericata,” Cellular and Molecular Life Sciences, vol. 67, no. 3, pp. 455–466, 2010. View at Publisher · View at Google Scholar · View at Scopus
  143. A. S. Andersen, D. Sandvang, K. M. Schnorr et al., “A novel approach to the antimicrobial activity of maggot debridement therapy,” Journal of Antimicrobial Chemotherapy, vol. 65, no. 8, pp. 1646–1654, 2010. View at Publisher · View at Google Scholar · View at Scopus
  144. S. Chernysh, S. I. Kim, G. Bekker et al., “Antiviral and antitumor peptides from insects,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 20, pp. 12628–12632, 2002. View at Publisher · View at Google Scholar · View at Scopus
  145. A. Bexfield, Y. Nigam, S. Thomas, and N. A. Ratcliffe, “Detection and partial characterisation of two antibacterial factors from the excretions/secretions of the medicinal maggot Lucilia sericata and their activity against methicillin-resistant Staphylococcus aureus (MRSA),” Microbes and Infection, vol. 6, no. 14, pp. 1297–1304, 2004. View at Publisher · View at Google Scholar · View at Scopus
  146. G. Telford, A. P. Brown, A. Kind, J. S. C. English, and D. I. Pritchard, “Maggot chymotrypsin I from Lucilia sericata is resistant to endogenous wound protease inhibitors,” British Journal of Dermatology, vol. 164, no. 1, pp. 192–196, 2011. View at Publisher · View at Google Scholar · View at Scopus
  147. M. J. A. van der Plas, G. N. Jukema, S.-W. Wai et al., “Maggot excretions/secretions are differentially effective against biofilms of Staphylococcus aureus and Pseudomonas aeruginosa,” Journal of Antimicrobial Chemotherapy, vol. 61, no. 1, pp. 117–122, 2008. View at Publisher · View at Google Scholar · View at Scopus
  148. L. G. Harris, A. Bexfield, Y. Nigam, H. Rohde, N. A. Ratcliffe, and D. Mack, “Disruption of Staphylococcus epidermidis biofilms by medicinal maggot Lucilia sericata excretions/secretions,” International Journal of Artificial Organs, vol. 32, no. 9, pp. 555–564, 2009. View at Google Scholar · View at Scopus
  149. B. Altincicek and A. Vilcinskas, “Septic injury-inducible genes in medicinal maggots of the green blow fly Lucilia sericata,” Insect Molecular Biology, vol. 18, no. 1, pp. 119–125, 2009. View at Publisher · View at Google Scholar · View at Scopus
  150. L. G. Harris, Y. Nigam, J. Sawyer et al., “Lucilia sericata chymotrypsin disrupts protein adhesin-mediated staphylococcal biofilm formation,” Applied and Environmental Microbiology, vol. 79, no. 4, pp. 1393–1395, 2013. View at Google Scholar
  151. Y. T. Pinilla, D. A. Moreno-Pérez, M. A. Patarroyo et al., “Proteolytic activity regarding Sarconesiopsis magellanica (Diptera:Calliphoridae) larval excretions and secretions,” Acta Tropica, vol. 128, pp. 686–691, 2013. View at Google Scholar
  152. A. G. Smith, R. A. Powis, D. I. Pritchard, and S. T. Britland, “Greenbottle (Lucilia sericata) larval secretions delivered from a prototype hydrogel wound dressing accelerate the closure of model wounds,” Biotechnology Progress, vol. 22, no. 6, pp. 1690–1696, 2006. View at Publisher · View at Google Scholar · View at Scopus
  153. D. I. Pritchard, G. Telford, M. Diab, and W. Low, “Expression of a cGMP compatible Lucilia sericata insect serine proteinase debridement enzyme,” Biotechnology Progress, vol. 28, no. 2, pp. 567–572, 2012. View at Publisher · View at Google Scholar · View at Scopus
  154. S. Britland, A. Smith, W. Finter et al., “Recombinant Lucilia sericata chymotrypsin in a topical hydrogel formulation degrades human wound eschar ex vivo,” Biotechnology Progress, vol. 27, no. 3, pp. 870–874, 2011. View at Publisher · View at Google Scholar · View at Scopus
  155. K. Zarchi and G. B. Jemec, “The efficacy of maggot debridement therapy—a review of comparative clinical trials,” International Wound Journal, vol. 9, no. 5, pp. 469–477, 2012. View at Publisher · View at Google Scholar · View at Scopus
  156. P. E. Prete, “Growth effects of Phaenicia sericata larval extracts on fibroblasts: mechanism for wound healing by maggot therapy,” Life Sciences, vol. 60, no. 8, pp. 505–510, 1997. View at Publisher · View at Google Scholar · View at Scopus
  157. X. Li, N. Liu, X. Xia et al., “The effects of maggot secretions on the inflammatory cytokines in serum of traumatic rats,” African Journal of Traditional and Complementary Alternative Medicine, vol. 10, no. 4, pp. 151–154, 2013. View at Google Scholar
  158. S. Natori, “Molecules participating in insect immunity of Sarcophaga peregrina,” Proceedings of the Japan Academy Series B: Physical and Biological Sciences, vol. 86, no. 10, pp. 927–938, 2010. View at Publisher · View at Google Scholar · View at Scopus
  159. V. Čeřovský, J. Slaninová, V. Fučík et al., “Lucifensin, a novel insect defensin of medicinal maggots: synthesis and structural study,” ChemBioChem, vol. 12, no. 9, pp. 1352–1361, 2011. View at Publisher · View at Google Scholar · View at Scopus
  160. B. El Shazely, V. Veverka, V. Fucik et al., “Lucifensin II, a defensin of medicinal maggots of the blowfly Lucilia cuprina (Diptera: Calliphoridae),” Journal of Medical Entomology, vol. 50, no. 3, pp. 571–578, 2013. View at Google Scholar
  161. I. Valachová, J. Bohová, Z. Pálošová et al., “Expression of lucifensin in Lucilia sericata medicinal maggots in infected environments,” Cell and Tissue Research, vol. 353, pp. 165–171, 2013. View at Google Scholar
  162. M. K. E. Nygaard, A. S. Andersen, H.-H. Kristensen, K. A. Krogfelt, P. Fojan, and R. Wimmer, “The insect defensin lucifensin from Lucilia sericata,” Journal of Biomolecular NMR, vol. 52, pp. 277–282, 2012. View at Publisher · View at Google Scholar · View at Scopus
  163. C. Joyner, M. K. Mills, and D. Nayduch, “Pseudomonas aeruginosa in Musca domestica L.: temporospatial examination of bacteria population dynamics and house fly antimicrobial responses,” PLoS ONE, vol. 8, no. 11, Article ID e79224, 2013. View at Publisher · View at Google Scholar
  164. S. O. Park, J. H. Shin, W. K. Choi, B. S. Park, J. S. Oh, and A. Jang, “Antibacterial activity of house fly-maggot extracts against MRSA (Methicillin-resistant Staphylococcus aureus) and VRE (Vancomycin-resistant enterococci),” Journal of Environmental Biology, vol. 31, no. 5, pp. 865–871, 2010. View at Google Scholar · View at Scopus
  165. S. Chernysh, K. Irina, and A. Irina, “Anti-tumor activity of immunomodulatory peptide alloferon-1 in mouse tumor transplantation model,” International Immunopharmacology, vol. 12, no. 1, pp. 312–314, 2012. View at Publisher · View at Google Scholar · View at Scopus
  166. S. Chernysh and I. Kozuharova, “Anti-tumor activity of a peptide combining patterns of insect alloferons and mammalian immunoglobulins in naïve and tumor antigen vaccinated mice,” International Immunopharmacology, vol. 17, pp. 1090–1093, 2013. View at Publisher · View at Google Scholar
  167. M.-J. Ryu, V. Anikin, S.-H. Hong et al., “Activation of NF-κB by alloferon through down-regulation of antioxidant proteins and IκBα,” Molecular and Cellular Biochemistry, vol. 313, no. 1-2, pp. 91–102, 2008. View at Publisher · View at Google Scholar · View at Scopus
  168. M. Kuczer, A. Midak-Siewirska, R. Zahorska, M. Łuczak, and D. Konopińska, “Further studies on the antiviral activity of alloferon and its analogues,” Journal of Peptide Science, vol. 17, no. 11, pp. 715–719, 2011. View at Publisher · View at Google Scholar · View at Scopus
  169. N. Lee, S. Bae, H. Kim et al., “Inhibition of lytic reactivation of Kaposi's sarcoma-associated herpesvirus by alloferon,” Antiviral Therapy, vol. 16, no. 3, pp. 439–442, 2011. View at Publisher · View at Google Scholar · View at Scopus
  170. G. R. Erdmann, “Antibacterial action of Myiasis-causing flies,” Parasitology Today, vol. 3, no. 7, pp. 214–216, 1987. View at Google Scholar · View at Scopus
  171. A. Kerridge, H. Lappin-Scott, and J. R. Stevens, “Antibacterial properties of larval secretions of the blowfly, Lucilia sericata,” Medical and Veterinary Entomology, vol. 19, no. 3, pp. 333–337, 2005. View at Publisher · View at Google Scholar · View at Scopus
  172. T. J. Graetz, B. R. Tellor, J. R. Smith, and M. S. Avidan, “Desirudin: a review of the pharmacology and clinical application for the prevention of deep vein thrombosis,” Expert Review of Cardiovascular Therapy, vol. 9, no. 9, pp. 1101–1109, 2011. View at Publisher · View at Google Scholar · View at Scopus
  173. M. Kazimírová and I. Štibrániova, “Tick salivary compounds: their role in modulation of host defences and pathogen transmission,” Cellular and Infection Microbiology, vol. 3, article 43, 2013. View at Publisher · View at Google Scholar
  174. J. M. C. Ribeiro, B. J. Mans, and B. Arcà, “An insight into the sialome of blood-feeding Nematocera,” Insect Biochemistry and Molecular Biology, vol. 40, no. 11, pp. 767–784, 2010. View at Publisher · View at Google Scholar · View at Scopus
  175. A. C. Figueiredo, D. de Sanctis, R. Gutiérrez-Gallego et al., “Unique thrombin-inhibition mechanism by anophelin, an anticoagulant from the malaria vector,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 52, pp. E3649–E3658, 2012. View at Publisher · View at Google Scholar