Beyond the venom: Exploring the antimicrobial peptides from Androctonus species of scorpion.
Androctonus species
antimicrobial peptides
scorpion
therapeutic potentials
venom
Journal
Journal of peptide science : an official publication of the European Peptide Society
ISSN: 1099-1387
Titre abrégé: J Pept Sci
Pays: England
ID NLM: 9506309
Informations de publication
Date de publication:
15 May 2024
15 May 2024
Historique:
revised:
12
04
2024
received:
04
01
2024
accepted:
01
05
2024
medline:
16
5
2024
pubmed:
16
5
2024
entrez:
15
5
2024
Statut:
aheadofprint
Résumé
Prevalent worldwide, the Androctonus scorpion genus contributes a vital role in scorpion envenoming. While diverse scorpionisms are observed because of several different species, their secretions to protect themselves have been identified as a potent source of antimicrobial peptide (AMP)-like compounds. Distinctly, the venom of these species contains around 24 different AMPs, with definite molecules studied for their therapeutic potential as antimicrobial, antifungal, antiproliferative and antiangiogenic agents. Our review focuses on the therapeutic potential of native and synthetic AMPs identified so far in the Androctonus scorpion genus, identifying research gaps in peptide therapeutics and guiding further investigations. Certain AMPs have demonstrated remarkable compatibility to be prescribed as anticancer drug to reduce cancer cell proliferation and serve as a potent antibiotic alternative. Besides, analyses were performed to explore the characteristics and affinities of peptides for membranes. Overall, the study of AMPs derived from the Androctonus scorpion genus provides valuable insights into their potential applications in medicine and drug development.
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e3613Informations de copyright
© 2024 European Peptide Society and John Wiley & Sons Ltd.
Références
Corrêa JAF, Evangelista AG, de Melo Nazareth T, Luciano FB. Fundamentals on the molecular mechanism of action of antimicrobial peptides. Materialia. 2019;8:100494. doi:10.1016/j.mtla.2019.100494
Tanwar J, Das S, Fatima Z, Hameed S. Multidrug resistance: an emerging crisis. Interdiscip Perspect Infect Dis. 2014;2014:e541340. doi:10.1155/2014/541340
Erdem Büyükkiraz M, Kesmen Z. Antimicrobial peptides (AMPs): a promising class of antimicrobial compounds. J Appl Microbiol. 2022;132(3):1573‐1596. doi:10.1111/jam.15314
Magana M, Pushpanathan M, Santos AL, et al. The value of antimicrobial peptides in the age of resistance. Lancet Infect Dis. 2020;20(9):e216‐e230. doi:10.1016/S1473‐3099(20)30327‐3
Pirtskhalava M, Amstrong AA, Grigolava M, et al. DBAASP v3: database of antimicrobial/cytotoxic activity and structure of peptides as a resource for development of new therapeutics. Nucleic Acids Res. 2021;49(D1):D288‐D297. doi:10.1093/nar/gkaa991
Shi G, Kang X, Dong F, et al. DRAMP 3.0: an enhanced comprehensive data repository of antimicrobial peptides. Nucleic Acids Res. 2022;50(D1):D488‐D496. doi:10.1093/nar/gkab651
The Nobel Prize in Physiology or Medicine 1945. NobelPrizeorg. Accessed June 20, 2023. https://www.nobelprize.org/prizes/medicine/1945/fleming/lecture/
de Kraker MEA, Stewardson AJ, Harbarth S. Will 10 million people die a year due to antimicrobial resistance by 2050? PLoS Med. 2016;13(11):e1002184. doi:10.1371/journal.pmed.1002184
Nikaido H. Multidrug resistance in bacteria. Annu Rev Biochem. 2009;78(1):119‐146. doi:10.1146/annurev.biochem.78.082907.145923
Silen W, Machen TE, Forte JG. Acid‐base balance in amphibian gastric mucosa. Am J Physiol. 1975;229(3):721‐730. doi:10.1152/ajplegacy.1975.229.3.721
Desales‐Salazar E, Khusro A, Cipriano‐Salazar M, Barbabosa‐Pliego A, Rivas‐Caceres RR. Scorpion venoms and associated toxins as anticancer agents: update on their application and mechanism of action. J Appl Toxicol. 2020;40(10):1310‐1324. doi:10.1002/jat.3976
Hmed B, Serria HT, Mounir ZK. Scorpion peptides: potential use for new drug development. J Toxicol. 2013;2013:1‐15. doi:10.1155/2013/958797
Ahmadi S, Knerr JM, Argemi L, et al. Scorpion venom: detriments and benefits. Biomedicine. 2020;8(5):118. doi:10.3390/biomedicines8050118
Tawfik MM, Bertelsen M, Abdel‐Rahman MA, Strong PN, Miller K. Scorpion venom antimicrobial peptides induce siderophore biosynthesis and oxidative stress responses in Escherichia coli. mSphere. 2021;6(3). doi:10.1128/msphere.00267‐21
Nasr S, Borges A, Sahyoun C, et al. Scorpion venom as a source of antimicrobial peptides: overview of biomolecule separation, analysis and characterization methods. Antibiotics. 2023;12(9):9. doi:10.3390/antibiotics12091380
Liu G, Yang F, Li F, et al. Therapeutic potential of a scorpion venom‐derived antimicrobial peptide and its homologs against antibiotic‐resistant gram‐positive bacteria. Front Microbiol. 2018;9:1159. doi:10.3389/fmicb.2018.01159
New report calls for urgent action to avert antimicrobial resistance crisis. Accessed June 20, 2023. https://www.who.int/news/item/29-04-2019-new-report-calls-for-urgent-action-to-avert-antimicrobial-resistance-crisis
Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002;415(6870):389‐395. doi:10.1038/415389a
Zhang C, Yang M. Antimicrobial peptides: from design to clinical application. Antibiotics. 2022;11(3):349. doi:10.3390/antibiotics11030349
Rodríguez AA, Otero‐González A, Ghattas M, Ständker L. Discovery, optimization, and clinical application of natural antimicrobial peptides. Biomedicine. 2021;9(10):1381. doi:10.3390/biomedicines9101381
Wu D, Fu L, Wen W, Dong N. The dual antimicrobial and immunomodulatory roles of host defense peptides and their applications in animal production. J Anim Sci Biotechnol. 2022;13(1):141. doi:10.1186/s40104‐022‐00796‐y
Browne K, Chakraborty S, Chen R, et al. A new era of antibiotics: the clinical potential of antimicrobial peptides. IJMS 2020;21(19):7047. doi:10.3390/ijms21197047
Madani F, Lindberg S, Langel Ü, Futaki S, Gräslund A. Mechanisms of cellular uptake of cell‐penetrating peptides. J Biophys. 2011;2011:e414729. doi:10.1155/2011/414729
Gordon YJ, Romanowski EG, McDermott AM. A review of antimicrobial peptides and their therapeutic potential as anti‐infective drugs. Curr Eye Res. 2005;30(7):505‐515. doi:10.1080/02713680590968637
Lai Y, Gallo RL. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 2009;30(3):131‐141. doi:10.1016/j.it.2008.12.003
Braff MH, Gallo RL. Antimicrobial peptides: an essential component of the skin defensive barrier. Curr Top Microbiol Immunol. 2006;306:91‐110. doi:10.1007/3‐540‐29916‐5_4
Otvos L Jr. Antibacterial peptides and proteins with multiple cellular targets. J Pept Sci. 2005;11(11):697‐706. doi:10.1002/psc.698
Mookherjee N, Lippert DND, Hamill P, et al. Intracellular receptor for human host defense peptide LL‐37 in monocytes. J Immunol. 2009;183(4):2688‐2696. doi:10.4049/jimmunol.0802586
Pushpanathan M, Gunasekaran P, Rajendhran J. Antimicrobial peptides: versatile biological properties. Int J Pept. 2013;2013:e675391. doi:10.1155/2013/675391
Ramesh S, Govender T, Kruger HG, de la Torre BG, Albericio F. Short antimicrobial peptides (SAMPs) as a class of extraordinary promising therapeutic agents. J Pept Sci. 2016;22(7):438‐451. doi:10.1002/psc.2894
Kumar P, Kizhakkedathu JN, Straus SK. Antimicrobial peptides: diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo. Biomolecules. 2018;8(1):4. doi:10.3390/biom8010004
Lei J, Sun L, Huang S, et al. The antimicrobial peptides and their potential clinical applications. Am J Transl Res. 2019;11(7):3919‐3931.
Talapko J, Meštrović T, Juzbašić M, et al. Antimicrobial peptides—mechanisms of action, antimicrobial effects and clinical applications. Antibiotics. 2022;11(10):1417. doi:10.3390/antibiotics11101417
Boparai JK, Sharma PK. Mini review on antimicrobial peptides, sources, mechanism and recent applications. Protein Pept Lett. 27(1):4‐16.
Moravej H, Moravej Z, Yazdanparast M, et al. Antimicrobial peptides: features, action, and their resistance mechanisms in bacteria. Microb Drug Resist. 2018;24(6):747‐767. doi:10.1089/mdr.2017.0392
Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS. Role of peptide hydrophobicity in the mechanism of action of α‐helical antimicrobial peptides. Antimicrob Agents Chemother. 2007;51(4):1398‐1406. doi:10.1128/aac.00925‐06
Luo Y, Song Y. Mechanism of antimicrobial peptides: antimicrobial, anti‐inflammatory and antibiofilm activities. Int J Mol Sci. 2021;22(21):11401. doi:10.3390/ijms222111401
Li J, Koh J‐J, Liu S, Lakshminarayanan R, Verma CS, Beuerman RW. Membrane active antimicrobial peptides: translating mechanistic insights to design. Front Neurosci. 2017;11:73. doi:10.3389/fnins.2017.00073
Raheem N, Straus SK. Mechanisms of action for antimicrobial peptides with antibacterial and antibiofilm functions. Front Microbiol. 2019;10:2866. doi:10.3389/fmicb.2019.02866
Huan Y, Kong Q, Mou H, Yi H. Antimicrobial peptides: classification, design, application and research progress in multiple fields. Front Microbiol. 2020;11:582779. doi:10.3389/fmicb.2020.582779
Wimley WC. Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chem Biol. 2010;5(10):905‐917. doi:10.1021/cb1001558
Singh T., P. Choudhary, S. Singh, T. Singh, P. Choudhary, and S. Singh, “Antimicrobial peptides: mechanism of action,” in Insights on Antimicrobial Peptides, IntechOpen, 2022. 10.5772/intechopen.99190.
Strandberg E, Schweigardt F, Wadhwani P, Ulrich AS. Mechanism of action of beta‐stranded antimicrobial (KL)n model peptides. Biophys J. 2023;122(3):369a. doi:10.1016/j.bpj.2022.11.2033
Oren Z, Shai Y. Mode of action of linear amphipathic α‐helical antimicrobial peptides. Pept Sci. 1998;47(6):451‐463. doi:10.1002/(SICI)1097‐0282(1998)47:6<451::AID‐BIP4>3.0.CO;2‐F
Lyu Y, Fitriyanti M, Narsimhan G. Nucleation and growth of pores in 1,2‐dimyristoyl‐sn‐glycero‐3‐phosphocholine (DMPC)/cholesterol bilayer by antimicrobial peptides melittin, its mutants and cecropin P1. Colloids Surf B Biointerfaces. 2019;173:121‐127. doi:10.1016/j.colsurfb.2018.09.049
Gazit E, Miller IR, Biggin PC, Sansom MSP, Shai Y. Structure and orientation of the mammalian antibacterial peptide Cecropin P1 within phospholipid membranes. J Mol Biol. 1996;258(5):860‐870. doi:10.1006/jmbi.1996.0293
Chen R, Mark AE. The effect of membrane curvature on the conformation of antimicrobial peptides: implications for binding and the mechanism of action. Eur Biophys J. 2011;40(4):545‐553. doi:10.1007/s00249‐011‐0677‐4
Sato H, Feix JB. Peptide–membrane interactions and mechanisms of membrane destruction by amphipathic α‐helical antimicrobial peptides. Biochim Biophys Acta BBA ‐ Biomembr. 2006;1758(9):1245‐1256. doi:10.1016/j.bbamem.2006.02.021
Matsuzaki K, Nakamura A, Murase O, Sugishita K, Fujii N, Miyajima K. Modulation of magainin 2‐lipid bilayer interactions by peptide charge. Biochemistry. 1997;36(8):2104‐2111. doi:10.1021/bi961870p
Matsuzaki K, Murase O, Miyajima K. Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers. Biochemistry. 1995;34(39):12553‐12559. doi:10.1021/bi00039a009
Imura Y, Choda N, Matsuzaki K. Magainin 2 in action: distinct modes of membrane Permeabilization in living bacterial and mammalian cells. Biophys J. 2008;95(12):5757‐5765. doi:10.1529/biophysj.108.133488
Lohner K, Prossnigg F. Biological activity and structural aspects of PGLa interaction with membrane mimetic systems. Biochim Biophys Acta. 2009;1788(8):1656‐1666. doi:10.1016/j.bbamem.2009.05.012
Sengupta D, Leontiadou H, Mark AE, Marrink S‐J. Toroidal pores formed by antimicrobial peptides show significant disorder. Biochim Biophys Acta BBA ‐ Biomembr. 2008;1778(10):2308‐2317. doi:10.1016/j.bbamem.2008.06.007
Kabelka I, Vácha R. Advances in molecular understanding of α‐helical membrane‐active peptides. Acc Chem Res. 2021;54(9):2196‐2204. doi:10.1021/acs.accounts.1c00047
Last NB, Schlamadinger DE, Miranker AD. A common landscape for membrane‐active peptides. Protein Sci Publ Protein Soc. 2013;22(7):870‐882. doi:10.1002/pro.2274
Tuerkova A, Kabelka I, Králová T, et al. Effect of helical kink in antimicrobial peptides on membrane pore formation. eLife. 2020;9:e47946. doi:10.7554/eLife.47946
Qian S, Wang W, Yang L, Huang HW. Structure of the alamethicin pore reconstructed by X‐ray diffraction analysis. Biophys J. 2008;94(9):3512‐3522. doi:10.1529/biophysj.107.126474
Hall JE, Vodyanoy I, Balasubramanian TM, Marshall GR. Alamethicin. A rich model for channel behavior. Biophys J. 1984;45(1):233‐247. doi:10.1016/S0006‐3495(84)84151‐X
Yang L, Harroun TA, Weiss TM, Ding L, Huang HW. Barrel‐stave model or toroidal model? A case study on melittin pores. Biophys J. 2001;81(3):1475‐1485. doi:10.1016/S0006‐3495(01)75802‐X
Ozkan O, Kar S, Güven E, Ergun G. Comparison of proteins, lethality and immunogenic compounds of Androctonus crassicauda (Olivier, 1807) (Scorpiones: Buthidae) venom obtained by different methods. J Venom Anim Toxins Trop Dis. 2007;13(4):844‐856. doi:10.1590/S1678‐91992007000400013
Ma R, Kwok HF. New opportunities and challenges of venom‐based and bacteria‐derived molecules for anticancer targeted therapy. Semin Cancer Biol. 2022;80:356‐369. doi:10.1016/j.semcancer.2020.08.010
Xia Z, He D, Wu Y, Kwok HF, Cao Z. Scorpion venom peptides: molecular diversity, structural characteristics, and therapeutic use from channelopathies to viral infections and cancers. Pharmacol Res. 2023;197:106978. doi:10.1016/j.phrs.2023.106978
Zuo W, Kwok HF. Design of bioengineered peptides/proteases as anti‐cancer reagents with integrated omics and machine learning approaches. In: Santamaria S, ed. Proteases and Cancer: Methods and Protocols. Methods in Molecular Biology. Springer US; 2024:295‐309. doi:10.1007/978‐1‐0716‐3589‐6_22
Ma R, Wong SW, Ge L, Shaw C, Siu SWI, Kwok HF. In vitro and MD simulation study to explore physicochemical parameters for antibacterial peptide to become potent anticancer peptide. Mol Ther ‐ Oncolytics. 2020;16:7‐19. doi:10.1016/j.omto.2019.12.001
Cesa‐Luna C, Muñoz‐Rojas J, Saab‐Rincon G, et al. Structural characterization of scorpion peptides and their bactericidal activity against clinical isolates of multidrug‐resistant bacteria. PLoS ONE. 2019;14(11):e0222438. doi:10.1371/journal.pone.0222438
Tripathi JK, Kathuria M, Kumar A, Mitra K, Ghosh JK. An unprecedented alteration in mode of action of IsCT resulting its translocation into bacterial cytoplasm and inhibition of macromolecular syntheses. Sci Rep. 2015;5:9127. doi:10.1038/srep09127
Chippaux J‐P, Goyffon M. Epidemiology of scorpionism: a global appraisal. Acta Trop. 2008;107(2):71‐79. doi:10.1016/j.actatropica.2008.05.021
Estrada‐Gómez S, Gomez‐Rave L, Vargas‐Muñoz LJ, van der Meijden A. Characterizing the biological and biochemical profile of six different scorpion venoms from the Buthidae and Scorpionidae family. Toxicon. 2017;130:104‐115. doi:10.1016/j.toxicon.2017.02.007
Laustsen AH, Solà M, Jappe EC, Oscoz S, Lauridsen LP, Engmark M. Biotechnological trends in spider and scorpion antivenom development. Toxins. 2016;8(8):226. doi:10.3390/toxins8080226
Ward MJ, Ellsworth SA, Nystrom GS. A global accounting of medically significant scorpions: epidemiology, major toxins, and comparative resources in harmless counterparts. Toxicon. 2018;151:137‐155. doi:10.1016/j.toxicon.2018.07.007
Almaaytah A, Zhou M, Wang L, Chen T, Walker B, Shaw C. Antimicrobial/cytolytic peptides from the venom of the North African scorpion, Androctonus amoreuxi: biochemical and functional characterization of natural peptides and a single site‐substituted analog. Peptides. 2012;35(2):291‐299. doi:10.1016/j.peptides.2012.03.016
Yang Y, Zeng X‐C, Zhang L, Nie Y, Shi W, Liu Y. Androcin, a novel type of cysteine‐rich venom peptide from Androctonus bicolor, induces akinesia and anxiety‐like symptoms in mice. IUBMB Life. 2014;66(4):277‐285. doi:10.1002/iub.1261
du Q, Hou X, Wang L, et al. AaeAP1 and AaeAP2: novel antimicrobial peptides from the venom of the scorpion, Androctonus aeneas: structural characterisation, molecular cloning of biosynthetic precursor‐encoding cDNAs and engineering of analogues with enhanced antimicrobial and anticancer activities. Toxins. 2015;7(2):219‐237. doi:10.3390/toxins7020219
Al‐Asmari AK, Riyasdeen A, Abbasmanthiri R, Arshaduddin M, Al‐Harthi FA. Scorpion (Androctonus bicolor) venom exhibits cytotoxicity and induces cell cycle arrest and apoptosis in breast and colorectal cancer cell lines. Indian J Pharmacol. 2016;48(5):537‐543. doi:10.4103/0253‐7613.190742
Su Y, Nishimoto T, Hoffman S, Nguyen X‐X, Pilewski JM, Feghali‐Bostwick C. Insulin‐like growth factor binding protein‐4 exerts antifibrotic activity by reducing levels of connective tissue growth factor and the C‐X‐C chemokine receptor 4. FASEB BioAdv. 2019;1(3):167‐179. doi:10.1096/fba.2018‐00015
Zhang L, Shi W, Zeng XC, et al. Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis. J Proteomics. 2015;128:231‐250. doi:10.1016/j.jprot.2015.07.030
Zargan J, Sajad M, Umar S, Naime M, Ali S, Khan HA. Scorpion (Androctonus crassicauda) venom limits growth of transformed cells (SH‐SY5Y and MCF‐7) by cytotoxicity and cell cycle arrest. Exp Mol Pathol. 2011;91(1):447‐454. doi:10.1016/j.yexmp.2011.04.008
Mikaelian AG, Traboulay E, Zhang XM, et al. Pleiotropic anticancer properties of scorpion venom peptides: Rhopalurus princeps venom as an anticancer agent. Drug des Devel Ther. 2020;14:881‐893. doi:10.2147/DDDT.S231008
Bayatzadeh MA, Zare Mirakabadi A, Babaei N, Doulah A, Doosti A. Expression and purification of recombinant alpha‐toxin AnCra1 from the scorpion Androctonus crassicauda and its functional characterization on mammalian sodium channels. Mol Biol Rep. 2021;48(9):6303‐6312. doi:10.1007/s11033‐021‐06624‐2
Wu Y, Ma H, Zhang F, Zhang C, Zou X, Cao Z. Selective voltage‐gated sodium channel peptide toxins from animal venom: pharmacological probes and analgesic drug development. ACS Chem Nerosci. 2018;9(2):187‐197. doi:10.1021/acschemneuro.7b00406
Caliskan F, Ergene E, Sogut I, et al. Biological assays on the effects of Acra3 peptide from Turkish scorpion Androctonus crassicauda venom on a mouse brain tumor cell line (BC3H1) and production of specific monoclonal antibodies. Toxicon. 2013;76:350‐361. doi:10.1016/j.toxicon.2013.09.009
Caliskan F, García BI, Coronas FIV, et al. Purification and cDNA cloning of a novel neurotoxic peptide (Acra3) from the scorpion Androctonus crassicauda. Peptides. 2012;37(1):106‐112. doi:10.1016/j.peptides.2012.07.009
Snyder SS, Gleaton JW, Kirui D, Chen W, Millenbaugh NJ. Antifungal activity of synthetic scorpion venom‐derived peptide analogues against Candida albicans. Int J Pept Res Ther. 2021;27(1):281‐291. doi:10.1007/s10989‐020‐10084‐w
du Q, Hou X, Ge L, et al. Cationicity‐enhanced analogues of the antimicrobial peptides, AcrAP1 and AcrAP2, from the venom of the scorpion, Androctonus crassicauda, display potent growth modulation effects on human cancer cell lines. Int J Biol Sci. 2014;10(10):1097‐1107. doi:10.7150/ijbs.9859
Salem ML, Shoukry NM, Teleb WK, Abdel‐Daim MM, Abdel‐Rahman MA. In vitro and in vivo antitumor effects of the Egyptian scorpion Androctonus amoreuxi venom in an Ehrlich ascites tumor model. SpringerPlus. 2016;5(1):570. doi:10.1186/s40064‐016‐2269‐3
Hosseinzadeh H, Zarei H, Taghiabadi E. Antinociceptive, anti‐inflammatory and acute toxicity effects of Juglans regia L. leaves in mice. Iran Red Crescent Med J. 2011;13(1):27‐33.
Akef H, Kotb N, Abo‐Elmatty D, Salem S. Anti‐proliferative effects of Androctonus amoreuxi scorpion and Cerastes snake venoms on human prostate cancer cells. J Cancer Prev. 2017;22(1):40‐46. doi:10.15430/JCP.2017.22.1.40
Nadjia B, Fatima L‐D. Beneficial effects of Androctonus australis hector venom and its non‐toxic fraction in the restoration of early hepatocyte‐carcinogenesis induced by FB1 mycotoxin: involvement of oxidative biomarkers. Exp Mol Pathol. 2015;99(2):198‐206. doi:10.1016/j.yexmp.2015.06.022
Bremnes RM, Camps C, Sirera R. Angiogenesis in non‐small cell lung cancer: the prognostic impact of neoangiogenesis and the cytokines VEGF and bFGF in tumours and blood. Lung Cancer. 2006;51(2):143‐158. doi:10.1016/j.lungcan.2005.09.005
Almaaytah A, Tarazi S, Abu‐Alhaijaa A, et al. Enhanced antimicrobial activity of AamAP1‐lysine, a novel synthetic peptide analog derived from the scorpion venom peptide AamAP1. Pharmaceuticals. 2014;7(5):502‐516. doi:10.3390/ph7050502
el‐Bitar AM, Sarhan MM, Aoki C, et al. Virocidal activity of Egyptian scorpion venoms against hepatitis C virus. Virol J. 2015;12(1):47. doi:10.1186/s12985‐015‐0276‐6
da Mata ÉCG, Mourão CBF, Rangel M, Schwartz EF. Antiviral activity of animal venom peptides and related compounds. J Venom Anim Toxins Trop Dis. 2017;23(1):3. doi:10.1186/s40409‐016‐0089‐0
Nafie MS, Abdel Daim MM, Ali IAI, Nabil ZI, Tantawy MA, Abdel‐Rahman MA. Antitumor efficacy of the Egyptian scorpion venom Androctonus Australis: in vitro and in vivo study. J Basic Appl Zool. 2020;81(1):8. doi:10.1186/s41936‐020‐00147‐1
Rjeibi I, Mabrouk K, Mosrati H, et al. Purification, synthesis and characterization of AaCtx, the first chlorotoxin‐like peptide from Androctonus australis scorpion venom. Peptides. 2011;32(4):656‐663. doi:10.1016/j.peptides.2011.01.015
Dardevet L, Rani D, Aziz T, et al. Chlorotoxin: a helpful natural scorpion peptide to diagnose glioma and fight tumor invasion. Toxins. 2015;7(4):1079‐1101. doi:10.3390/toxins7041079
Lyons SA, O'Neal J, Sontheimer H. Chlorotoxin, a scorpion‐derived peptide, specifically binds to gliomas and tumors of neuroectodermal origin. Glia. 2002;39(2):162‐173. doi:10.1002/glia.10083
Ehret‐Sabatier L, Loew D, Goyffon M, et al. Characterization of novel cysteine‐rich antimicrobial peptides from scorpion blood *. J Biol Chem. 1996;271(47):29537‐29544. doi:10.1074/jbc.271.47.29537
Mandard N, Sy D, Maufrais C, et al. Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: solution structure and molecular dynamics simulations in the presence of a lipid monolayer. J Biomol Struct Dyn. 1999;17(2):367‐380. doi:10.1080/07391102.1999.10508368
Hetru C, Letellier L, Oren Z, Hoffmann JA, Shai Y. Androctonin, a hydrophilic disulphide‐bridged non‐haemolytic anti‐microbial peptide: a plausible mode of action. Biochem J. 2000;345(3):653‐664. doi:10.1042/bj3450653
Boldt K, Rist W, Weiss SM, Weith A, Lenter MC. FPRL‐1 induces modifications of migration‐associated proteins in human neutrophils. Proteomics. 2006;6(17):4790‐4799. doi:10.1002/pmic.200600121
Almaaytah A, Tarazi S, Mhaidat N, Al‐Balas Q, Mukattash TL. Mauriporin, a novel aationic α‐helical pptide with selective cytotoxic activity against prostate cancer cell lines from the venom of the scorpion androctonus mauritanicus. Int J Pept Res Ther. 2013;19(4):281‐293. doi:10.1007/s10989‐013‐9350‐3
Almaaytah A, Tarazi S, Alsheyab F, Al‐Balas Q, Mukattash T. Antimicrobial and antibiofilm activity of mauriporin, a multifunctional scorpion venom peptide. Int J Pept Res Ther. 2014;20(4):397‐408. doi:10.1007/s10989‐014‐9405‐0
Yang C‐H, Chen YC, Peng SY, et al. An engineered arginine‐rich α‐helical antimicrobial peptide exhibits broad‐spectrum bactericidal activity against pathogenic bacteria and reduces bacterial infections in mice. Sci Rep. 2018;8(1):14602. doi:10.1038/s41598‐018‐32981‐3
Deslouches B, Montelaro RC, Urish KL, Di YP. Engineered cationic antimicrobial peptides (eCAPs) to combat multidrug‐resistant bacteria. Pharmaceutics. 2020;12(6):501. doi:10.3390/pharmaceutics12060501
Almaaytah A, Abualhaijaa A, Alqudah O. The evaluation of the synergistic antimicrobial and antibiofilm activity of AamAP1‐lysine with conventional antibiotics against representative resistant strains of both gram‐positive and gram‐negative bacteria. Infect Drug Resist. 2019;12:1371‐1380. doi:10.2147/IDR.S204626
Satitmanwiwat S, Changsangfa C, Khanuengthong A, et al. The scorpion venom peptide BmKn2 induces apoptosis in cancerous but not in normal human oral cells. Biomed Pharmacother Biomedecine Pharmacother. 2016;84:1042‐1050. doi:10.1016/j.biopha.2016.10.041
Panja K, Buranapraditkun S, Roytrakul S, et al. Scorpion venom peptide effects on inhibiting proliferation and inducing apoptosis in canine mammary gland tumor cell lines. Animals. 2021;11(7):2119. doi:10.3390/ani11072119
Midura‐Nowaczek K, Markowska A. Antimicrobial peptides and their analogs: searching for new potential therapeutics. Perspect Med Chem. 2014;6:PMC.S13280. doi:10.4137/PMC.S13215
Wang G, Li X, Wang Z. APD3: the antimicrobial peptide database as a tool for research and education. Nucleic Acids Res. 2016;44(D1):D1087‐D1093. doi:10.1093/nar/gkv1278
Gondane AA, Pawar DB. Activity of cefotaxime versus ceftriaxone against pathogens isolated from various systemic infections: a prospective, multicenter, comparative, in vitro indian study. J Lab Physicians 2023;s‐0043‐1772564. doi:10.1055/s‐0043‐1772564
Azevedo AC, Bizerra FC, da Matta DA, de Almeida LP, Rosas R, Colombo AL. In vitro susceptibility of a large collection of Candida strains against fluconazole and voriconazole by using the CLSI disk diffusion assay. Mycopathologia. 2011;171(6):411‐416. doi:10.1007/s11046‐010‐9387‐1
Shen Y, Maupetit J, Derreumaux P, Tufféry P. Improved PEP‐FOLD approach for peptide and miniprotein structure prediction. J Chem Theory Comput. 2014;10(10):4745‐4758. doi:10.1021/ct500592m
Alland C, Moreews F, Boens D, et al. RPBS: a web resource for structural bioinformatics. Nucleic Acids Res. 2005;33(Web Server):W44‐W49. doi:10.1093/nar/gki477
Roy A, Kucukural A, Zhang Y. I‐TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc. 2010;5:725‐738. doi:10.1038/nprot.2010.5
Sievers F, Higgins DG. Clustal omega for making accurate alignments of many protein sequences. Protein Sci. 2018;27(1):135‐145. doi:10.1002/pro.3290
Edgar RC, Batzoglou S. Multiple sequence alignment. Curr Opin Struct Biol. 2006;16(3):368‐373. doi:10.1016/j.sbi.2006.04.004
Gasteiger E, Hoogland C, Gattiker A, et al. Protein identification and analysis tools on the ExPASy Server. In: Walker JM, ed. The Proteomics Protocols Handbook. in Springer Protocols Handbooks. Humana Press; 2005:571‐607. doi:10.1385/1–59259–890‐0:571
Gupta S, Kapoor P, Chaudhary K, et al. In silico approach for predicting toxicity of peptides and proteins. PLoS ONE. 2013;8(9):e73957. doi:10.1371/journal.pone.0073957
He J, Luo X, Jin D, Wang Y, Zhang T. Identification, recombinant expression, and characterization of LGH2, a novel antimicrobial peptide of lactobacillus casei HZ1. Molecules. 2018;23(9):2246. doi:10.3390/molecules23092246
Ji D, Udenigwe CC, Agyei D. Antioxidant peptides encrypted in flaxseed proteome: an in silico assessment. Food Sci Human Wellness. 2019;8(3):306‐314. doi:10.1016/j.fshw.2019.08.002
Lomize AL, Todd SC, Pogozheva ID. Spatial arrangement of proteins in planar and curved membranes by PPM 3.0. Protein Sci. 2022;31(1):209‐220. doi:10.1002/pro.4219
Lomize MA, Pogozheva ID, Joo H, Mosberg HI, Lomize AL. OPM database and PPM web server: resources for positioning of proteins in membranes. Nucleic Acids Res. 2012;40(D1):D370‐D376. doi:10.1093/nar/gkr703