Skip to content
2000
image of The Dual Nature of Venom: Transforming Toxins into Therapeutic Peptides

Abstract

Venom has been extracted from venomous animals since ancient times for use as hunting tools or biological weapons. In the modern era, the focus has shifted toward the biomedical potential of venom, particularly its rich composition of bioactive compounds. Among these, venom peptides are of particular interest due to their potent and selective biological activities. These peptides often constitute a significant portion of crude venom mixtures and have emerged as promising candidates for drug development. The growing body of research in this field has led to the establishment of “venomics,” a discipline that integrates proteomics, transcriptomics, and genomics to comprehensively characterize venom components. Technological advancements, such as high-throughput sequencing, mass spectrometry, and advanced computational tools, have revolutionized venomics, enabling deeper insights into venom composition, function, and evolutionary biology. These innovations have facilitated the discovery of venom-derived peptides with therapeutic applications, including treatments for chronic pain, cancer, cardiovascular diseases, and autoimmune disorders. However, despite these promising developments, challenges remain. These include the complexity of venom mixtures, ethical considerations in venom collection, and difficulties in translating findings into clinical applications. This review explores the evolution and technological progress of venomics, highlights key therapeutic applications of venom peptides, and discusses current limitations and future prospects in the field.

© 2026 Bentham Science Publishers
Loading

Article metrics loading...

/content/journals/ppl/10.2174/0109298665429958251204082928
2026-02-10
2026-03-11

  • From This Site

    /content/journals/ppl/10.2174/0109298665429958251204082928
    dcterms_title,dcterms_subject,pub_keyword
    -contentType:Contributor -contentType:Concept -contentType:Institution
    10
    5
Loading full text...

Full text loading...

References

  1. Lewis R.J. Garcia M.L. Therapeutic potential of venom peptides. Nat. Rev. Drug Discov. 2003 2 10 790 802 10.1038/nrd1197 14526382
    [Google Scholar]
  2. Vidya V. Achar R.R. Venom peptides: A comprehensive translational perspective in pain management. Curr. Res. Toxicol. 2021 2 329 340 10.1016/j.crtox.2021.09.001
    [Google Scholar]
  3. Nicolau C.A. Carvalho P.C. Junqueira-de-Azevedo I.L.M. Teixeira-Ferreira A. Junqueira M. Perales J. Neves-Ferreira A.G.C. Valente R.H. An in-depth snake venom proteopeptidome characterization: Benchmarking Bothrops jararaca. J. Proteomics 2017 151 214 231 10.1016/j.jprot.2016.06.029 27373870
    [Google Scholar]
  4. Pennington M.W. Czerwinski A. Norton R.S. Peptide therapeutics from venom: Current status and potential. Bioorg. Med. Chem. 2018 26 10 2738 2758 10.1016/j.bmc.2017.09.029 28988749
    [Google Scholar]
  5. Peter Muiruri K. Zhong J. Yao B. Lai R. Luo L. Bioactive peptides from scorpion venoms: therapeutic scaffolds and pharmacological tools. Chin. J. Nat. Med. 2023 21 1 19 35 10.1016/S1875‑5364(23)60382‑6 36641229
    [Google Scholar]
  6. a Suhas R. Structure, function and mechanistic aspects of scorpion venom peptides - A boon for the development of novel therapeutics. Eur. J. Med. Chem. Rep. 2022 6 100068 10.1016/j.ejmcr.2022.100068
    [Google Scholar]
  7. b Soon T.N. Chia A.Y.Y. Yap W.H. Tang Y.Q. Anticancer Mechanisms of Bioactive Peptides. Protein Pept. Lett. 2020 27 9 823 830 10.2174/0929866527666200409102747 32271692
    [Google Scholar]
  8. a Slagboom J. Kaal C. Arrahman A. Vonk F.J. Somsen G.W. Calvete J.J. Wüster W. Kool J. Analytical strategies in venomics. Microchem. J. 2022 175 107187 10.1016/j.microc.2022.107187
    [Google Scholar]
  9. b Otvos R. A. Heus F. Vonk F. J. Halff J. Bruyneel B. Paliukhovich I. Smit A. B. Niessen W. M. Kool J. Analytical workflow for rapid screening and purification of bioactives from venom proteomes. Toxicon 2013 76 270 281 10.1016/j.toxicon.2013.10.013 24140918
    [Google Scholar]
  10. Dutertre S. Venomics in medicinal chemistry. Future Med. Chem. 2014 6 15 1609 1610 25406000
    [Google Scholar]
  11. Kaas Q. Craik D. Bioinformatics-Aided Venomics. Toxins (Basel) 2015 7 6 2159 2187 10.3390/toxins7062159 26110505
    [Google Scholar]
  12. Abd El-Aziz T.M. Soares A.G. Stockand J.D. Advances in venomics: Modern separation techniques and mass spectrometry. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2020 1160 122352 10.1016/j.jchromb.2020.122352 32971366
    [Google Scholar]
  13. Kulbacka J. Choromańska A. Rossowska J. Weżgowiec J. Saczko J. Rols M.P. Cell Membrane Transport Mechanisms: Ion Channels and Electrical Properties of Cell Membranes. Adv. Anat. Embryol. Cell Biol. 2017 227 39 58 10.1007/978‑3‑319‑56895‑9_3 28980039
    [Google Scholar]
  14. Dutertre S. Lewis R.J. Use of venom peptides to probe ion channel structure and function. J. Biol. Chem. 2010 285 18 13315 13320 10.1074/jbc.R109.076596 20189991
    [Google Scholar]
  15. Bhandari P. Computational strategies for designing peptide therapeutics with high binding affinity and stability. Int. Rev. Exp. Sci. Discov. Technol. Adv. 2024 8 11
    [Google Scholar]
  16. Alewood P. Mobli M. King G. The structural universe of disulfide-rich venom peptides. Venoms to Drugs Royal Society of Chemistry 2015 37 79 10.1039/9781849737876‑00037
    [Google Scholar]
  17. Wulff H. Christophersen P. Colussi P. Chandy K.G. Yarov-Yarovoy V. Antibodies and venom peptides: New modalities for ion channels. Nat. Rev. Drug Discov. 2019 18 5 339 357 10.1038/s41573‑019‑0013‑8 30728472
    [Google Scholar]
  18. Catterall W.A. Voltage-gated calcium channels. Cold Spring Harb. Perspect. Biol. 2011 3 8 a003947 10.1101/cshperspect.a003947 21746798
    [Google Scholar]
  19. Lewis R.J. Nielsen K.J. Craik D.J. Loughnan M.L. Adams D.A. Sharpe I.A. Luchian T. Adams D.J. Bond T. Thomas L. Jones A. Matheson J.L. Drinkwater R. Andrews P.R. Alewood P.F. Novel omega-conotoxins from Conus catus discriminate among neuronal calcium channel subtypes. J. Biol. Chem. 2000 275 45 35335 35344 10.1074/jbc.M002252200 10938268
    [Google Scholar]
  20. Morales Duque H. Campos Dias S. Franco O. Structural and functional analyses of Cone Snail toxins. Mar. Drugs 2019 17 6 370 10.3390/md17060370 31234371
    [Google Scholar]
  21. García M.C. Hernández-Gallegos Z. Escamilla J. Sánchez J.A. Calciseptine, a Ca2+ channel blocker, has agonist actions on L-type Ca2+ currents of frog and mammalian skeletal muscle. J. Membr. Biol. 2001 184 2 121 129 10.1007/s00232‑001‑0080‑7 11719849
    [Google Scholar]
  22. Meitzler J.L. Hinde S. Bánfi B. Nauseef W.M. Ortiz de Montellano P.R. Conserved cysteine residues provide a protein-protein interaction surface in dual oxidase (DUOX) proteins. J. Biol. Chem. 2013 288 10 7147 7157 10.1074/jbc.M112.414797 23362256
    [Google Scholar]
  23. Wang J. Ou S.W. Wang Y.J. Distribution and function of voltage-gated sodium channels in the nervous system. Channels (Austin) 2017 11 6 534 554 28922053
    [Google Scholar]
  24. Rodríguez de la Vega R. C. Possani L. D. Overview of scorpion toxins specific for Na+ channels and related peptides: Biodiversity, structure–function relationships and evolution. Toxicon 2005 46 8 831 844 10.1016/j.toxicon.2005.09.006 16274721
    [Google Scholar]
  25. Zhang Y. Zhang L. Fan X. Yang W. Yu B. Kou J. Li F. Captopril attenuates TAC-induced heart failure via inhibiting Wnt3a/β-catenin and Jak2/Stat3 pathways. Biomed. Pharmacother. 2019 113 108780 10.1016/j.biopha.2019.108780 30889487
    [Google Scholar]
  26. George K. Lopez-Mateos D. Abd El-Aziz T.M. Xiao Y. Kline J. Bao H. Raza S. Stockand J.D. Cummins T.R. Fornelli L. Rowe M.P. Yarov-Yarovoy V. Rowe A.H. Structural and functional characterization of a novel scorpion toxin that inhibits NaV1.8 via interactions with the DI voltage sensor and DII pore module. Front. Pharmacol. 2022 13 846992 35662692
    [Google Scholar]
  27. Lee C.W. Bae C. Lee J. Ryu J.H. Kim H.H. Kohno T. Swartz K.J. Kim J.I. Solution structure of kurtoxin: a gating modifier selective for Cav3 voltage-gated Ca(2+) channels. Biochemistry 2012 51 9 1862 1873 10.1021/bi201633j 22329781
    [Google Scholar]
  28. Montandon G.G. Cassoli J.S. Peigneur S. Verano-Braga T. Santos D.M. Paiva A.L.B. Moraes É.R. Kushmerick C. Borges M.H. Richardson M. Pimenta A.M.C. Kjeldsen F. Diniz M.R.V. Tytgat J. Lima M.E. GiTx1(β/κ-theraphotoxin-Gi1a), a novel toxin from the venom of Brazilian tarantula Grammostola iheringi (Mygalomorphae, Theraphosidae): Isolation, structural assessments and activity on voltage-gated ion channels. Biochimie 2020 176 138 149 10.1016/j.biochi.2020.07.008 32717411
    [Google Scholar]
  29. Lawrence N. Wu B. Ligutti J. Cheneval O. Agwa A.J. Benfield A.H. Biswas K. Craik D.J. Miranda L.P. Henriques S.T. Schroeder C.I. Peptide-membrane interactions affect the inhibitory potency and selectivity of spider toxins ProTx-II and GpTx-1. ACS Chem. Biol. 2019 14 1 118 130 10.1021/acschembio.8b00989 30507158
    [Google Scholar]
  30. Wang Z. Sang M. Zhang Y. Chen S. Li S. Chen Y. Xu E. Zhou Q. Xu W. Zhao C. Wang D. Lu W. Cao P. BmKK2, a thermostable Kv1.3 blocker from Buthus martensii Karsch (BmK) scorpion, inhibits the activation of macrophages via Kv1.3-NF-κB- NLRP3 axis. J. Ethnopharmacol. 2023 314 116624 10.1016/j.jep.2023.116624 37182676
    [Google Scholar]
  31. Zhang N. Chen X. Li M. Cao C. Wang Y. Wu G. Hu G. Wu H. Solution structure of BmKK4, the first member of subfamily alpha-KTx 17 of scorpion toxins. Biochemistry 2004 43 39 12469 12476 10.1021/bi0490643 15449936
    [Google Scholar]
  32. Mouhat S. De Waard M. Sabatier J.M. Contribution of the functional dyad of animal toxins acting on voltage‐gated Kv1‐type channels. J. Pept. Sci. 2005 11 2 65 68 10.1002/psc.630 15635666
    [Google Scholar]
  33. Novoseletsky V.N. Volyntseva A.D. Shaitan K.V. Kirpichnikov M.P. Feofanov A.V. Modeling of the binding of peptide blockers to voltage-gated potassium channels: Approaches and evidence. Acta Nat. (Engl. Ed.) 2016 8 2 35 46 10.32607/20758251‑2016‑8‑2‑35‑46 27437138
    [Google Scholar]
  34. Féger J. Gil-Falgon S. Lamaze C. Cell receptors: Definition, mechanisms and regulation of receptor-mediated endocytosis. Cell. Mol. Biol. 1994 40 8 1039 1061 7873978
    [Google Scholar]
  35. a Kampo S. Cui Y. Yu J. Anabah T.W. Falagán A.A. Bayor M.T. Wen Q.P. Scorpion Venom peptide, AGAP inhibits TRPV1 and potentiates the analgesic effect of lidocaine. Heliyon 2021 7 12 e08560 10.1016/j.heliyon.2021.e08560 35005265
    [Google Scholar]
  36. b Jergova S. Perez C. Imperial J.S. Gajavelli S. Jain A. Abin A. Olivera B.M. Sagen J. Cannabinoid receptor agonists from Conus venoms alleviate pain-related behavior in rats. Pharmacol. Biochem. Behav. 2021 205 173182 10.1016/j.pbb.2021.173182 33774007
    [Google Scholar]
  37. Van Baelen A.C. Robin P. Kessler P. Maïga A. Gilles N. Servent D. Structural and Functional Diversity of Animal Toxins Interacting With GPCRs. Front. Mol. Biosci. 2022 9 811365 10.3389/fmolb.2022.811365 35198603
    [Google Scholar]
  38. Hwang S.M. Jo Y.Y. Cohen C.F. Kim Y.H. Berta T. Park C.K. Venom Peptide Toxins Targeting the Outer Pore Region of Transient Receptor Potential Vanilloid 1 in Pain: Implications for Analgesic Drug Development. Int. J. Mol. Sci. 2022 23 10 5772 10.3390/ijms23105772 35628583
    [Google Scholar]
  39. Ghazal A. Clarke D. Abdel-Rahman M.A. Ribeiro A. Collie-Duguid E. Pattinson C. Burgoyne K. Muhammad T. Alfadhel S. Heidari Z. Samir R. Gerges M.M. Nkene I. Colamarino R.A. Hijazi K. Houssen W.E. Venomous gland transcriptome and venom proteomic analysis of the scorpion Androctonus amoreuxi reveal new peptides with anti-SARS-CoV-2 activity. Peptides 2024 173 171139 10.1016/j.peptides.2023.171139 38142817
    [Google Scholar]
  40. a Ramirez-Acosta K. Rosales-Fuerte I.A. Perez-Sanchez J.E. Nuñez-Rivera A. Juarez J. Cadena-Nava R.D. Design and selection of peptides to block the SARS-CoV-2 receptor binding domain by molecular docking. Beilstein J. Nanotechnol. 2022 13 699 711 10.3762/bjnano.13.62 35957673
    [Google Scholar]
  41. b Chun C.Y. Khor S.X.Y. Chia A.Y.Y. Tang Y.Q. In silico study of potential SARS-CoV-2 antagonist from Clitoria ternatea. Int. J. Health Sci. (Qassim) 2023 17 3 3 10 37151745
    [Google Scholar]
  42. Johansson-Åkhe I. Wallner B. Improving peptide-protein docking with AlphaFold-Multimer using forced sampling. Front. Bioinform. 2022 2 959160 10.3389/fbinf.2022.959160 36304330
    [Google Scholar]
  43. Belkheir K. Laref N. The inhibitory effect of vitamins on O micron virus via targeting the ACE2 receptor. In silico analysis. J. King Saud Univ. Sci. 2024 36 2 103082
    [Google Scholar]
  44. Arpornsuwan T. Sriwai W. Jaresitthikunchai J. Phaonakrop N. Sritanaudomchai H. Roytrakul S. Anticancer activities of antimicrobial BmKn2 peptides against oral and colon cancer cells. Int. J. Pept. Res. Ther. 2014 20 4 501 509 10.1007/s10989‑014‑9417‑9
    [Google Scholar]
  45. Robinson P.K. Enzymes: principles and biotechnological applications. Essays Biochem. 2015 59 1 41 10.1042/bse0590001 26504249
    [Google Scholar]
  46. a Miyamoto J.G. Kitano E.S. Zelanis A. Nachtigall P.G. Junqueira-de-Azevedo I. Sant’Anna S.S. Lauria da Silva R. Bersanetti P.A. Carmona A.K. Barbosa Pereira P.J. Serrano S.M.T. Vilela Oliva M.L. Tashima A.K. A novel metalloproteinase-derived cryptide from Bothrops cotiara venom inhibits angiotensin-converting enzyme activity. Biochimie 2024 216 90 98 10.1016/j.biochi.2023.10.010 37839625
    [Google Scholar]
  47. b Pinheiro-Júnior E.L. Boldrini-França J. de Campos Araújo L.M.P. Santos-Filho N.A. Bendhack L.M. Cilli E.M. Arantes E.C. LmrBPP9: A synthetic bradykinin-potentiating peptide from Lachesis muta rhombeata venom that inhibits the angiotensin-converting enzyme activity in vitro and reduces the blood pressure of hypertensive rats. Peptides 2018 102 1 7 10.1016/j.peptides.2018.01.015 29410030
    [Google Scholar]
  48. c Hayashi M. A. Camargo A. C. The Bradykinin-potentiating peptides from venom gland and brain of Bothrops jararaca contain highly site specific inhibitors of the somatic angiotensin-converting enzyme. Toxicon 2005 45 8 1163
    [Google Scholar]
  49. Sciani J.M. Pimenta D.C. The modular nature of bradykinin-potentiating peptides isolated from snake venoms. J. Venom. Anim. Toxins Incl. Trop. Dis. 2017 23 1 45 10.1186/s40409‑017‑0134‑7 29090005
    [Google Scholar]
  50. Cho A.E. Rinaldo D. Extension of QM/MM docking and its applications to metalloproteins. J. Comput. Chem. 2009 30 16 2609 2616 10.1002/jcc.21270 19373896
    [Google Scholar]
  51. Matsuzaki K. Membrane Permeabilization Mechanisms. Adv. Exp. Med. Biol. 2019 1117 9 16 10.1007/978‑981‑13‑3588‑4_2 30980350
    [Google Scholar]
  52. a Wen X. Gongpan P. Meng Y. Nieh J. C. Yuan H. Tan K. Functional characterization, antimicrobial effects, and potential antibacterial mechanisms of new mastoparan peptides from hornet venom (Vespa ducalis, Vespa mandarinia, and Vespa affinis). Toxicon 2021 200 48 54 10.1016/j.toxicon.2021.07.001 34237341
    [Google Scholar]
  53. b Jeon E. Kim M.K. Park Y. Efficacy of the bee-venom antimicrobial peptide Osmin against sensitive and carbapenem-resistant Klebsiella pneumoniae strains. Int. J. Antimicrob. Agents 2024 63 2 107054 10.1016/j.ijantimicag.2023.107054 38072166
    [Google Scholar]
  54. c Tan L. Bai L. Wang L. He L. Li G. Du W. Shen T. Xiang Z. Wu J. Liu Z. Hu M. Antifungal activity of spider venom-derived peptide lycosin-I against Candida tropicalis. Microbiol. Res. 2018 216 120 128 10.1016/j.micres.2018.08.012 30269852
    [Google Scholar]
  55. a Bastos V. Pascoal S. Lopes K. Mortari M. Oliveira H. Cytotoxic effects of Chartergellus communis wasp venom peptide against melanoma cells. Biochimie 2024 216 99 107 10.1016/j.biochi.2023.10.015 37879427
    [Google Scholar]
  56. b Marinho A. D. Lucena da Silva E. Jullyanne de Sousa Portilho A. Lacerda Brasil de Oliveira L. Cintra Austregésilo Bezerra E. Maria Dias Nogueira B. Leitão-Araújo M. Lúcia Machado-Alves M. Correa Neto C. Seabra Ferreira R. Jr de Fátima Aquino Moreira-Nunes C. Elisabete Amaral de Moraes M. Jorge R. J. B. Montenegro R. C. Three snake venoms from Bothrops genus induced apoptosis and cell cycle arrest in K562 human leukemic cell line. Toxicon 2024 238 107547
    [Google Scholar]
  57. c Thakur R. Kini S. Kurkalang S. Banerjee A. Chatterjee P. Chanda A. Chatterjee A. Panda D. Mukherjee A.K. Mechanism of apoptosis induction in human breast cancer MCF-7 cell by Ruviprase, a small peptide from Daboia russelii russelii venom. Chem. Biol. Interact. 2016 258 297 304 10.1016/j.cbi.2016.09.004 27613483
    [Google Scholar]
  58. d Satitmanwiwat S. Changsangfa C. Khanuengthong A. Promthep K. Roytrakul S. Arpornsuwan T. Saikhun K. Sritanaudomchai H. The scorpion venom peptide BmKn2 induces apoptosis in cancerous but not in normal human oral cells. Biomed. Pharmacother. 2016 84 1042 1050 10.1016/j.biopha.2016.10.041 27780132
    [Google Scholar]
  59. Adams D.J. Berecki G. Mechanisms of conotoxin inhibition of N-type (Cav2.2) calcium channels. Biochim. Biophys. Acta Biomembr. 2013 1828 7 1619 1628 10.1016/j.bbamem.2013.01.019 23380425
    [Google Scholar]
  60. Zhang F. Zhang C. Xu X. Zhang Y. Gong X. Yang Z. Zhang H. Tang D. Liang S. Liu Z. Naja atra venom peptide reduces pain by selectively blocking the voltage-gated sodium channel Nav1.8. J. Biol. Chem. 2019 294 18 7324 7334 10.1074/jbc.RA118.007370 30804211
    [Google Scholar]
  61. Kampo S. Ahmmed B. Zhou T. Owusu L. Anabah T.W. Doudou N.R. Kuugbee E.D. Cui Y. Lu Z. Yan Q. Wen Q.P. Scorpion venom analgesic peptide, BmK AGAP inhibits stemness, and epithelial-mesenchymal transition by down-regulating PTX3 in breast cancer. Front. Oncol. 2019 9 21 10.3389/fonc.2019.00021 30740360
    [Google Scholar]
  62. Ianzer D. Santos R.A.S. Etelvino G.M. Xavier C.H. de Almeida Santos J. Mendes E.P. Machado L.T. Prezoto B.C. Dive V. de Camargo A.C.M. Do the cardiovascular effects of angiotensin-converting enzyme (ACE) I involve ACE-independent mechanisms? new insights from proline-rich peptides of Bothrops jararaca. J. Pharmacol. Exp. Ther. 2007 322 2 795 805 10.1124/jpet.107.120873 17475904
    [Google Scholar]
  63. El-Seedi H. Abd El-Wahed A. Yosri N. Musharraf S.G. Chen L. Moustafa M. Zou X. Al-Mousawi S. Guo Z. Khatib A. Khalifa S. Antimicrobial properties of Apis mellifera’s Bee venom. Toxins 2020 12 7 451 10.3390/toxins12070451 32664544
    [Google Scholar]
  64. Ren Y. Li C. Chang J. Wang R. Wang Y. Chu X.P. Hi1a as a novel neuroprotective agent for ischemic stroke by inhibition of acid-sensing ion channel 1a. Transl. Stroke Res. 2018 9 2 96 98 10.1007/s12975‑017‑0575‑x 29027122
    [Google Scholar]
  65. Mobli M. Undheim E.A.B. Rash L.D. Modulation of ion channels by cysteine-rich peptides. Adv. Pharmacol. 2017 79 199 223 10.1016/bs.apha.2017.03.001 28528669
    [Google Scholar]
  66. Conceição K. Santos J.M. Bruni F.M. Klitzke C.F. Marques E.E. Borges M.H. Melo R.L. Fernandez J.H. Lopes-Ferreira M. Characterization of a new bioactive peptide from Potamotrygon gr. orbignyi freshwater stingray venom. Peptides 2009 30 12 2191 2199 10.1016/j.peptides.2009.08.004 19682520
    [Google Scholar]
  67. Cushman D.W. Ondetti M.A. Design of angiotensin converting enzyme inhibitors. Nat. Med. 1999 5 10 1110 1112 10.1038/13423 10502801
    [Google Scholar]
  68. Curran M.P. Keating G.M. Eptifibatide. Drugs 2005 65 14 2009 2035 10.2165/00003495‑200565140‑00007 16162023
    [Google Scholar]
  69. Miljanich G.P. Ziconotide: Neuronal calcium channel blocker for treating severe chronic pain. Curr. Med. Chem. 2004 11 23 3029 3040 15578997
    [Google Scholar]
  70. Furman B. L. The development of Byetta (exenatide) from the venom of the Gila monster as an anti-diabetic agent. Toxicon 2012 59 4 464 471 10.1016/j.toxicon.2010.12.016 21194543
    [Google Scholar]
  71. Memariani H. Memariani M. Moravvej H. Shahidi-Dadras M. Melittin: A venom-derived peptide with promising anti-viral properties. Eur. J. Clin. Microbiol. Infect. Dis. 2020 39 1 5 17 10.1007/s10096‑019‑03674‑0 31422545
    [Google Scholar]
  72. Zhang Z. Bao X. Li D. Batroxobin inhibits astrocyte activation following nigrostriatal pathway injury. Neural Regen. Res. 2021 16 4 721 726 33063734
    [Google Scholar]
  73. Trim S.A. Trim C.M. Venom: The sharp end of pain therapeutics. Br. J. Pain 2013 7 4 179 188 26516522
    [Google Scholar]
  74. Yam M.F. Loh Y.C. Tan C.S. Khadijah Adam S. Abdul Manan N. Basir R. General pathways of pain sensation and the major neurotransmitters involved in pain regulation. Int. J. Mol. Sci. 2018 19 8 2164 30042373
    [Google Scholar]
  75. Jami S. Erickson A. Brierley S.M. Vetter I. Pain-causing venom peptides: Insights into sensory neuron pharmacology. Toxins 2017 10 1 15 29280959
    [Google Scholar]
  76. Henriques S.T. Deplazes E. Lawrence N. Cheneval O. Chaousis S. Inserra M. Thongyoo P. King G.F. Mark A.E. Vetter I. Craik D.J. Schroeder C.I. Interaction of tarantula venom peptide ProTx-II with lipid membranes is a prerequisite for its inhibition of human voltage-gated sodium channel NaV1.7. J. Biol. Chem. 2016 291 33 17049 17065 27311819
    [Google Scholar]
  77. Gonçalves T.C. Benoit E. Partiseti M. Servent D. The NaV1.7 channel subtype as an antinociceptive target for spider toxins in adult dorsal root ganglia neurons. Front. Pharmacol. 2018 9 1000 30233376
    [Google Scholar]
  78. Pinheiro-Junior E.L. Alirahimi E. Peigneur S. Isensee J. Schiffmann S. Erkoc P. Fürst R. Vilcinskas A. Sennoner T. Koludarov I. Hempel B.F. Tytgat J. Hucho T. von Reumont B.M. Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling. BMC Biol. 2024 22 1 164 39075558
    [Google Scholar]
  79. Sharma H. Swetanshu Singh P. Role of Yoga in Cardiovascular Diseases. Curr. Probl. Cardiol. 2024 49 1 Pt A 102032 37582455
    [Google Scholar]
  80. Kini R.M. Koh C.Y. Snake venom three-finger toxins and their potential in drug development targeting cardiovascular diseases. Biochem. Pharmacol. 2020 181 114105 32579959
    [Google Scholar]
  81. Ciolek J. Zoukimian C. Dhot J. Burban M. Triquigneaux M. Lauzier B. Guimbert C. Boturyn D. Ferron M. Ciccone L. Tepshi L. Stura E. Legrand P. Robin P. Mourier G. Schaack B. Fellah I. Blanchet G. Gauthier-Erfanian C. Beroud R. Servent D. De Waard M. Gilles N. MT9, a natural peptide from black mamba venom antagonizes the muscarinic type 2 receptor and reverses the M2R-agonist-induced relaxation in rat and human arteries. Biomedicine & pharmacotherapy 2022 150 113094
    [Google Scholar]
  82. Lumsden N.G. Khambata R.S. Hobbs A.J. C-type natriuretic peptide (CNP): Cardiovascular roles and potential as a therapeutic target. Curr. Pharm. Des. 2010 16 37 4080 4088 10.2174/138161210794519237 21247399
    [Google Scholar]
  83. Mirzaei S. Fekri H.S. Hashemi F. Hushmandi K. Mohammadinejad R. Ashrafizadeh M. Zarrabi A. Garg M. Venom peptides in cancer therapy: An updated review on cellular and molecular aspects. Pharmacol. Res. 2021 164 105327 10.1016/j.phrs.2020.105327 33276098
    [Google Scholar]
  84. a Hubalek M. Czech T. Müller H. Biological subtypes of triple-negative breast cancer. Breast Care 2017 12 1 8 14 10.1159/000455820 28611535
    [Google Scholar]
  85. b Yau A.W.N. Chu S.Y.C. Yap W.H. Wong C.L. Chia A.Y.Y. Tang Y.Q. Phage display screening in breast cancer: From peptide discovery to clinical applications. Life Sci. 2024 357 123077 10.1016/j.lfs.2024.123077 39332485
    [Google Scholar]
  86. Soares S. Lopes K. S. Mortari M. Oliveira H. Bastos V. Antitumoral potential of Chartergellus-CP1 peptide from Chartergellus communis wasp venom in two different breast cancer cell lines (HR+ and triple-negative). Toxicon 2022 216 148 156 10.1016/j.toxicon.2022.07.004 35839869
    [Google Scholar]
  87. Ghodeif S.K. El-Fahla N.A. Abdel-Rahman M.A. El-Shenawy N.S. Arthropod venom peptides: Pioneering nanotechnology in cancer treatment and drug delivery. Cancer Pathogenesis and Therapy In Press, Corrected Proof 2025
    [Google Scholar]
  88. Wasay M. Awan S. Shahbaz N. Khan S. Sher K. Malik A. Mustafa S. Siddiqi A.I. Barech S. Farooq A. Hameed S. Siddiqui M. Ahmad A. Asif A. Sherin A. Majid H. Nauman A. Soomro B. Subhan M. Rafique I. Saqib M.A.N. Neurological disorders and disability in Pakistan: A cross-sectional multicenter study. J. Neurol. Sci. 2023 452 120754 10.1016/j.jns.2023.120754 37562167
    [Google Scholar]
  89. Deplazes E. Molecular simulations of disulfide-rich venom peptides with ion channels and membranes. Molecules 2017 22 3 362 10.3390/molecules22030362 28264446
    [Google Scholar]
  90. Hernández-Sámano A.C. Falcón A. Zamudio F. Michel-Morfín J.E. Landa-Jaime V. López-Vera E. Jeziorski M.C. Aguilar M.B. A short framework-III (mini-M-2) conotoxin from the venom of a vermivorous species, Conus archon, inhibits human neuronal nicotinic acetylcholine receptors. Peptides 2022 153 170785 10.1016/j.peptides.2022.170785 35307452
    [Google Scholar]
  91. a Saez N. J. Herzig V. Versatile spider venom peptides and their medical and agricultural applications. Toxicon 2019 158 109 126 10.1016/j.toxicon.2018.11.298 30543821
    [Google Scholar]
  92. b Cardoso F.C. Pineda S.S. Herzig V. Sunagar K. Shaikh N.Y. Jin A.H. King G.F. Alewood P.F. Lewis R.J. Dutertre S. The deadly toxin arsenal of the tree-dwelling australian funnel-web spiders. Int. J. Mol. Sci. 2022 23 21 13077 10.3390/ijms232113077 36361863
    [Google Scholar]
  93. a Lopez S.M.M. Aguilar J.S. Fernandez J.B.B. Lao A.G.J. Estrella M.R.R. Devanadera M.K.P. Ramones C.M.V. Villaraza A.J.L. Guevarra L.A. Jr Santiago-Bautista M.R. Santiago L.A. Neuroactive venom compounds obtained from Phlogiellus bundokalbo as potential leads for neurodegenerative diseases: insights on their acetylcholinesterase and beta-secretase inhibitory activities in vitro. J. Venom. Anim. Toxins Incl. Trop. Dis. 2021 27 e20210009 10.1590/1678‑9199‑jvatitd‑2021‑0009 34249120
    [Google Scholar]
  94. b Lamptey R.N.L. Chaulagain B. Trivedi R. Gothwal A. Layek B. Singh J. A review of the common neurodegenerative disorders: current therapeutic approaches and the potential role of nanotherapeutics. Int. J. Mol. Sci. 2022 23 3 1851 10.3390/ijms23031851 35163773
    [Google Scholar]
  95. Decet M. Scott P. Kuenen S. Meftah D. Swerts J. Calatayud C. Gallego S.F. Kaempf N. Nachman E. Praschberger R. Schoovaerts N. Tang C.C. Eidelberg D. Al Adawi S. Al Asmi A. Nandhagopal R. Verstreken P. A candidate loss-of-function variant in SGIP1 causes synaptic dysfunction and recessive parkinsonism. Cell Rep. Med. 2024 5 10 101749 10.1016/j.xcrm.2024.101749 39332416
    [Google Scholar]
  96. Alberto-Silva C. Silva B. R. Molecular and cellular mechanisms of neuroprotection by oligopeptides from snake venoms. Biocell 2024 48 10.32604/biocell.2024.050443
    [Google Scholar]
  97. Martins N.M. Santos N.A.G. Sartim M.A. Cintra A.C.O. Sampaio S.V. Santos A.C. A tripeptide isolated from Bothrops atrox venom has neuroprotective and neurotrophic effects on a cellular model of Parkinson’s disease. Chem. Biol. Interact. 2015 235 10 16 10.1016/j.cbi.2015.04.004 25868679
    [Google Scholar]
  98. Yin S. M. Zhao D. Yu D. Q. Li S. L. An D. Peng Y. Xu H. Sun Y. P. Wang D. M. Zhao J. Zhang W. Q. Neuroprotection by scorpion venom heat resistant peptide in 6-hydroxydopamine rat model of early-stage Parkinson’s disease. Sheng Li Xue Bao 2014 66 6 658 666 25516514
    [Google Scholar]
  99. Ye M. Chung H.S. Lee C. Yoon M.S. Yu A.R. Kim J.S. Hwang D.S. Shim I. Bae H. Neuroprotective effects of bee venom phospholipase A2 in the 3xTg AD mouse model of Alzheimer’s disease. J. Neuroinflammation 2016 13 1 10 10.1186/s12974‑016‑0476‑z 26772975
    [Google Scholar]
  100. Nguyen C.D. Lee G. Neuroprotective activity of melittin—the main component of bee venom—against oxidative stress induced by Aβ25–35 in in vitro and in vivo models. Antioxidants 2021 10 11 1654 10.3390/antiox10111654 34829525
    [Google Scholar]
  101. Alberto-Silva C. Portaro F.C.V. Kodama R.T. Pantaleão H.Q. Rangel M. Nihei K. Konno K. Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis. J. Venom. Anim. Toxins Incl. Trop. Dis. 2021 27 e20200171 10.1590/1678‑9199‑jvatitd‑2020‑0171 34194483
    [Google Scholar]
  102. Hou K. Wu Z.X. Chen X.Y. Wang J.Q. Zhang D. Xiao C. Zhu D. Koya J.B. Wei L. Li J. Chen Z.S. Microbiota in health and diseases. Signal Transduct. Target. Ther. 2022 7 1 135 10.1038/s41392‑022‑00974‑4 35461318
    [Google Scholar]
  103. Ceremuga M. Stela M. Janik E. Gorniak L. Synowiec E. Sliwinski T. Sitarek P. Saluk-Bijak J. Bijak M. Melittin: A natural peptide from bee venom which induces apoptosis in human leukaemia cells. Biomolecules 2020 10 2 247 10.3390/biom10020247 32041197
    [Google Scholar]
  104. Ullah A. Aldakheel F. M. Anjum S. I. Raza G. Khan S. A. Tlak Gajger I. Pharmacological properties and therapeutic potential of honey bee venom. Saudi Pharm. J. 2023 31 1 96 109 10.1016/j.jsps.2022.11.008 36685303
    [Google Scholar]
  105. Chen Y. Cao L. Zhong M. Zhang Y. Han C. Li Q. Yang J. Zhou D. Shi W. He B. Liu F. Yu J. Sun Y. Cao Y. Li Y. Li W. Guo D. Cao Z. Yan H. Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7. PLoS One 2012 7 4 e34947 10.1371/journal.pone.0034947 22536342
    [Google Scholar]
  106. Gottler L.M. Ramamoorthy A. Structure, membrane orientation, mechanism, and function of pexiganan: A highly potent antimicrobial peptide designed from magainin. Biochim. Biophys. Acta Biomembr. 2009 1788 8 1680 1686 10.1016/j.bbamem.2008.10.009 19010301
    [Google Scholar]
  107. Dash R. Bhattacharjya S. Thanatin: An emerging host defense antimicrobial peptide with multiple modes of action. Int. J. Mol. Sci. 2021 22 4 1522 10.3390/ijms22041522 33546369
    [Google Scholar]
  108. Zhang S. Ma M. Shao Z. Zhang J. Fu L. Li X. Fang W. Gao L. Structure and Formation Mechanism of Antimicrobial Peptides Temporin B- and L-Induced Tubular Membrane Protrusion. Int. J. Mol. Sci. 2021 22 20 11015 10.3390/ijms222011015 34681675
    [Google Scholar]
  109. de Santana C.J.C. Pires Júnior O.R. Fontes W. Palma M.S. Castro M.S. Mastoparans: A Group of Multifunctional α-Helical Peptides With Promising Therapeutic Properties. Front. Mol. Biosci. 2022 9 824989 10.3389/fmolb.2022.824989 35813822
    [Google Scholar]
  110. Vernen F. Harvey P.J. Dias S.A. Veiga A.S. Huang Y.H. Craik D.J. Lawrence N. Troeira Henriques S. Characterization of tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties. Int. J. Mol. Sci. 2019 20 17 4184 10.3390/ijms20174184 31455019
    [Google Scholar]
  111. Gao X. Ding J. Liao C. Xu J. Liu X. Lu W. Defensins: The natural peptide antibiotic. Adv. Drug Deliv. Rev. 2021 179 114008 34673132
    [Google Scholar]
  112. Ghazvini K. Kamali H. Farsiani H. Yousefi M. Keikha M. Sustain-release lipid-liquid crystal formulations of pexiganan against Helicobacter pylori infection: in vitro evaluation in C57BL/6 mice. BMC Pharmacol. Toxicol. 2024 25 1 9 38212864
    [Google Scholar]
  113. Liu Y. Du Q. Ma C. Xi X. Wang L. Zhou M. Burrows J.F. Chen T. Wang H. Structure-activity relationship of an antimicrobial peptide, Phylloseptin-PHa: Balance of hydrophobicity and charge determines the selectivity of bioactivities. Drug Des. Devel. Ther. 2019 13 447 458 30774309
    [Google Scholar]
  114. Ilu A. Chia M. A. Cataldi T. R. Labate C. A. Ebiloma G. U. Yusuf P. O. Shuaibu M. N. Balogun E. O. Type I-like metalloproteinase in the venom of the West African saw-scaled carpet viper (Echis ocellatus) has anti-trypanosomal activity against African trypanosomes. Toxicon 2023 229 107138 10.1016/j.toxicon.2023.107138 37127124
    [Google Scholar]
  115. Freire K.A. Torres M.D.T. Lima D.B. Monteiro M.L. Bezerra de Menezes R.R.P.P. Martins A.M.C. Oliveira V.X. Jr Wasp venom peptide as a new antichagasic agent. Toxicon 2020 181 71 78 10.1016/j.toxicon.2020.04.099 32360153
    [Google Scholar]
  116. Rabea E.Y. Mahmoud E.D. Mohamed N.K. Ansary E.R. Alrouby M.R. Shehata R.R. Mokhtar Y.Y. Arullampalam P. Hegazy A.M. Al-Sabi A. Abd El-Aziz T.M. Potential of venom-derived compounds for the development of new antimicrobial agents. Toxins 2025 17 5 238 10.3390/toxins17050238 40423321
    [Google Scholar]
  117. HarveyA. L.Toxins and drug discovery.Toxicon20149219320010.1016/j.toxicon.2014.10.02025448391
     [Google Scholar]
  118. Herzig V. Cristofori-Armstrong B. Israel M.R. Nixon S.A. Vetter I. King G.F. Animal toxins — Nature’s evolutionary-refined toolkit for basic research and drug discovery. Biochem. Pharmacol. 2020 181 114096 10.1016/j.bcp.2020.114096 32535105
    [Google Scholar]
  119. Lameu C. Hayashi M.A.F. Guerreiro J.R. Oliveira E.F. Lebrun I. Pontieri V. Morais K.L.P. Camargo A.C.M. Ulrich H. The central nervous system as target for antihypertensive actions of a proline‐rich peptide from Bothrops jararaca venom. Cytometry A 2010 77A 3 220 230 10.1002/cyto.a.20860 20099250
    [Google Scholar]
  120. Ferreira S.H. From the Bothrops Jararaca Bradykinin Potentiating Peptides to Angiotensin Converting Enzyme Inhibitors. Toxins and Hemostasis: From Bench to Bedside. Kini R.M. Clemetson K.J. Markland F.S. McLane M.A. Morita T. Dordrecht Springer Netherlands 2010 13 17 10.1007/978‑90‑481‑9295‑3_2
    [Google Scholar]
  121. Diniz-Sousa R. Caldeira C.A.S. Pereira S.S. Da Silva S.L. Fernandes P.A. Teixeira L.M.C. Zuliani J.P. Soares A.M. Therapeutic applications of snake venoms: An invaluable potential of new drug candidates. Int. J. Biol. Macromol. 2023 238 124357 10.1016/j.ijbiomac.2023.124357 37028634
    [Google Scholar]
  122. Prashanth J.R. Hasaballah N. Vetter I. Pharmacological screening technologies for venom peptide discovery. Neuropharmacology 2017 127 4 19 10.1016/j.neuropharm.2017.03.038 28377116
    [Google Scholar]
  123. Tonin G. Klen J. Eptifibatide, an Older Therapeutic Peptide with New Indications: From Clinical Pharmacology to Everyday Clinical Practice. Int. J. Mol. Sci. 2023 24 6 5446 10.3390/ijms24065446 36982519
    [Google Scholar]
  124. Lazarovici P. Marcinkiewicz C. Lelkes P.I. From Snake Venom’s Disintegrins and C-Type Lectins to Anti-Platelet Drugs. Toxins (Basel) 2019 11 5 303 10.3390/toxins11050303 31137917
    [Google Scholar]
  125. Lambe T. Duarte R. Eldabe R. Copley S. Kansal A. Black S. Dupoiron D. Eldabe S. Ziconotide for the management of cancer pain: A budget impact analysis. Neuromodulation 2023 26 6 1226 1232 10.1016/j.neurom.2022.08.458 36202713
    [Google Scholar]
  126. Trevisan G. Oliveira S.M. Animal venom peptides cause antinociceptive effects by voltage-gated calcium channels activity blockage. Curr. Neuropharmacol. 2022 20 8 1579 1599 10.2174/1570159X19666210713121217 34259147
    [Google Scholar]
  127. Bentham Science Publisher B.S.P. Pharmacological inhibition of voltage-gated ca2+ channels for chronic pain relief. Curr. Neuropharmacol. 2013 11 6 606 620 10.2174/1570159X11311060005 24396337
    [Google Scholar]
  128. McGivern J.G. Ziconotide: A review of its pharmacology and use in the treatment of pain. Neuropsychiatr. Dis. Treat. 2007 3 1 69 85 10.2147/nedt.2007.3.1.69 19300539
    [Google Scholar]
  129. Chen Y. Shu A. Jiang M. Jiang J. Du Q. Chen T. Shaw C. Chai W. Chao T. Li X. Wu Q. Gao C. Exenatide improves hypogonadism and attenuates inflammation in diabetic mice by modulating gut microbiota. Int. Immunopharmacol. 2023 120 110339 10.1016/j.intimp.2023.110339 37210914
    [Google Scholar]
  130. Robinson S.D. Safavi-Hemami H. Venom peptides as pharmacological tools and therapeutics for diabetes. Neuropharmacology 2017 127 79 86 10.1016/j.neuropharm.2017.07.001 28689026
    [Google Scholar]
  131. Lodato M. Plaisance V. Pawlowski V. Kwapich M. Barras A. Buissart E. Dalle S. Szunerits S. Vicogne J. Boukherroub R. Abderrahmani A. Venom Peptides, polyphenols and alkaloids: Are they the next antidiabetics that will preserve β-cell mass and function in type 2 diabetes? Cells 2023 12 6 940 10.3390/cells12060940 36980281
    [Google Scholar]
  132. Williams J. A. GLP-1 mimetic drugs and the risk of exocrine pancreatic disease: Cell and animal studies. Pancreatology 2016 16 1 2 7 10.1016/j.pan.2015.11.008 26751948
    [Google Scholar]
  133. Romano J.D. Li H. Napolitano T. Realubit R. Karan C. Holford M. Tatonetti N.P. Discovering venom-derived drug candidates using differential gene expression. Toxins 2023 15 7 451 10.3390/toxins15070451 37505720
    [Google Scholar]
  134. Kerkkamp H. Bagowski C. Kool J. van Soolingen B. Vonk F. J. Vlecken D. Whole snake venoms: Cytotoxic, anti-metastatic and antiangiogenic properties. Toxicon 2018 150 39 49 10.1016/j.toxicon.2018.05.004 29763628
    [Google Scholar]
  135. Smallwood T.B. Clark R.J. Advances in venom peptide drug discovery: Where are we at and where are we heading? Expert Opin. Drug Discov. 2021 16 10 1163 1173 10.1080/17460441.2021.1922386 33914674
    [Google Scholar]
  136. Okkerse P. Hay J.L. Sitsen E. Dahan A. Klaassen E. Houghton W. Groeneveld G.J. Pharmacokinetics and pharmacodynamics of intrathecally administered Xen2174, a synthetic conopeptide with norepinephrine reuptake inhibitor and analgesic properties. Br. J. Clin. Pharmacol. 2017 83 4 751 763 10.1111/bcp.13176 27987228
    [Google Scholar]
  137. Rivera-de-Torre E. Rimbault C. Jenkins T.P. Sørensen C.V. Damsbo A. Saez N.J. Duhoo Y. Hackney C.M. Ellgaard L. Laustsen A.H. Strategies for heterologous expression, synthesis, and purification of animal venom toxins. Front. Bioeng. Biotechnol. 2022 9 811905 10.3389/fbioe.2021.811905 35127675
    [Google Scholar]
  138. Jenkins T.P. Laustsen A.H. Cost of manufacturing for recombinant snakebite antivenoms. Front. Bioeng. Biotechnol. 2020 8 703 32766215
    [Google Scholar]
  139. Scott D.A. Wright C.E. Angus J.A. Actions of intrathecal omega-conotoxins CVID, GVIA, MVIIA, and morphine in acute and neuropathic pain in the rat. Eur. J. Pharmacol. 2002 451 3 279 286 12242089
    [Google Scholar]
  140. Zhu Q. Chen Z. Paul P.K. Lu Y. Wu W. Qi J. Oral delivery of proteins and peptides: Challenges, status quo and future perspectives. Acta Pharm. Sin. B 2021 11 8 2416 2448 34522593
    [Google Scholar]
  141. Santhanakrishnan K.R. Koilpillai J. Narayanasamy D. PEGylation in pharmaceutical development: Current status and emerging trends in macromolecular and immunotherapeutic drugs. Cureus 2024 16 8 e66669 39262507
    [Google Scholar]
  142. Biessy L. Boundy M.J. Smith K.F. Harwood D.T. Hawes I. Wood S.A. Tetrodotoxin in marine bivalves and edible gastropods: A mini-review. Chemosphere 2019 236 124404 10.1016/j.chemosphere.2019.124404 31545201
    [Google Scholar]
  143. Whitelaw B.L. Cooke I.R. Finn J. Zenger K. Strugnell J.M. The evolution and origin of tetrodotoxin acquisition in the blue-ringed octopus (genus Hapalochlaena). Aquat. Toxicol. 2019 206 114 122 10.1016/j.aquatox.2018.10.012 30472480
    [Google Scholar]
  144. Melnikova D.I. Khotimchenko Y.S. Magarlamov T.Y. Addressing the Issue of Tetrodotoxin Targeting. Mar. Drugs 2018 16 10 352 10.3390/md16100352 30261623
    [Google Scholar]
  145. MacKenzie T.M.G. Abderemane-Ali F. Garrison C.E. Minor D.L. Jr Bois J.D. Differential effects of modified batrachotoxins on voltage-gated sodium channel fast and slow inactivation. Cell Chem. Biol. 2022 29 4 615 624.e5 10.1016/j.chembiol.2021.12.003 34963066
    [Google Scholar]
  146. Shiraishi Y. Ogawa T. Suzuki T. Iwai M. Kusano M. Zaitsu K. Kondo F. Ishii A. Seno H. Simultaneous quantification of batrachotoxin and epibatidine in plasma by ultra-performance liquid chromatography/tandem mass spectrometry. Leg. Med. (Tokyo) 2017 25 1 5 10.1016/j.legalmed.2016.12.008 28457503
    [Google Scholar]
  147. Hashemzadeh M. Furukawa M. Goldsberry S. Movahed M.R. Chemical structures and mode of action of intravenous glycoprotein IIb/IIIa receptor blockers: A review. Exp. Clin. Cardiol. 2008 13 4 192 197 19343166
    [Google Scholar]
  148. Jimenez E.C. Cruz L.J. Conotoxins as Tools in Research on Nicotinic Receptors. Toxins and Drug Discovery. Gopalakrishnakone P. Dordrecht Springer Netherlands 2015 1 17
    [Google Scholar]
  149. Brady R. Baell J. Norton R. Strategies for the development of conotoxins as new therapeutic leads. Mar. Drugs 2013 11 7 2293 2313 10.3390/md11072293 23812174
    [Google Scholar]
  150. Alves P. L. Abdalla F. M. F. Alponti R. F. Silveira P. F. Anti-obesogenic and hypolipidemic effects of a glucagon-like peptide-1 receptor agonist derived from the saliva of the Gila monster. Toxicon 2017 135 1 11 10.1016/j.toxicon.2017.06.001 28579479
    [Google Scholar]
  151. dos Santos A.P. de Araújo T.G. Rádis-Baptista G. Nanoparticles Functionalized with Venom-Derived Peptides and Toxins for Pharmaceutical Applications. Curr. Pharm. Biotechnol. 2020 21 2 97 109 10.2174/1389201020666190621104624 31223083
    [Google Scholar]
  152. Bhowmik T. Saha P.P. Dasgupta A. Gomes A. Antileukemic potential of PEGylated gold nanoparticle conjugated with protein toxin (NKCT1) isolated from Indian cobra (Naja kaouthia) venom. Cancer Nanotechnol. 2013 4 1-3 39 55 10.1007/s12645‑013‑0036‑5 26069500
    [Google Scholar]
  153. Ojeda P.G. Henriques S.T. Pan Y. Nicolazzo J.A. Craik D.J. Wang C.K. Lysine to arginine mutagenesis of chlorotoxin enhances its cellular uptake. Biopolymers 2017 108 5 e23025 10.1002/bip.23025 28459137
    [Google Scholar]
  154. Schlossbauer A. Dohmen C. Schaffert D. Wagner E. Bein T. pH-responsive release of acetal-linked melittin from SBA-15 mesoporous silica. Angew. Chem. Int. Ed. 2011 50 30 6828 6830 10.1002/anie.201005120 21688354
    [Google Scholar]
  155. Boaro A. Ageitos L. Torres M.D.T. Blasco E.B. Oztekin S. de la Fuente-Nunez C. Structure-function-guided design of synthetic peptides with anti-infective activity derived from wasp venom. Cell Rep. Phys. Sci. 2023 4 7 101459 10.1016/j.xcrp.2023.101459 38239869
    [Google Scholar]
  156. Ding X. Wang Y. Zhang S. Zhang R. Chen D. Chen L. Zhang Y. Luo S.Z. Xu J. Pei C. Self-assembly nanostructure of myristoylated ω-conotoxin MVIIA increases the duration of efficacy and reduces side effects. Mar. Drugs 2023 21 4 229 10.3390/md21040229 37103368
    [Google Scholar]
/content/journals/ppl/10.2174/0109298665429958251204082928
Loading
The Dual Nature of Venom: Transforming Toxins into Therapeutic Peptides
Bentham Science Publishers ; https://doi.org/10.2174/0109298665429958251204082928
/content/journals/ppl/10.2174/0109298665429958251204082928
/content/journals/ppl/10.2174/0109298665429958251204082928
Loading

Data & Media loading...


  • Article Type:     Review Article
Keywords: drug discovery ; biotechnology ; venomics ; Venom peptides ; proteomics ; therapeutic applications ; bioactive compounds

Most Cited Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test