{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T16:16:53Z","timestamp":1787242613712,"version":"build-2736575974"},"reference-count":42,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2024,4]]},"DOI":"10.1016\/j.toxicon.2024.107657","type":"journal-article","created":{"date-parts":[[2024,2,29]],"date-time":"2024-02-29T01:09:53Z","timestamp":1709168993000},"page":"107657","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"special_numbering":"C","title":["Characterization of an antimicrobial peptide family from the venom gland of Heteropoda venatoria"],"prefix":"10.1016","volume":"241","author":[{"given":"Zhihao","family":"Peng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chao","family":"Wei","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jisen","family":"Cai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhaoxia","family":"Zou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5495-051X","authenticated-orcid":false,"given":"Jinjun","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"3","key":"10.1016\/j.toxicon.2024.107657_bib1","doi-asserted-by":"crossref","DOI":"10.1007\/s13205-023-03512-3","article-title":"Cloning, recombinant expression, purification, and functional characterization of AGAAN antibacterial peptide","volume":"13","author":"Ajingi","year":"2023","journal-title":"3 Biotech"},{"issue":"1","key":"10.1016\/j.toxicon.2024.107657_bib2","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1074\/jbc.M114.595678","article-title":"Structure of membrane-active toxin from crab spider heriaeus melloteei suggests parallel evolution of Sodium channel gating modifiers in araneomorphae and mygalomorphae","volume":"290","author":"Berkut","year":"2015","journal-title":"J. Biol. Chem."},{"issue":"10","key":"10.1016\/j.toxicon.2024.107657_bib3","doi-asserted-by":"crossref","first-page":"3283","DOI":"10.1128\/AEM.02750-06","article-title":"Assessment and interpretation of bacterial viability by using the LIVE\/DEAD BacLight kit in combination with flow cytometry","volume":"73","author":"Berney","year":"2007","journal-title":"Appl. Environ. Microbiol."},{"issue":"12","key":"10.1016\/j.toxicon.2024.107657_bib4","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1002\/psc.2574","article-title":"The importance of being kinked: role of Pro residues in the selectivity of the helical antimicrobial peptide P5","volume":"19","author":"Bobone","year":"2013","journal-title":"J. Pept. Sci."},{"issue":"1","key":"10.1016\/j.toxicon.2024.107657_bib5","doi-asserted-by":"crossref","first-page":"4","DOI":"10.2174\/18755305MTAwENDE80","article-title":"Mini review on antimicrobial peptides, sources, mechanism and recent applications","volume":"27","author":"Boparai","year":"2020","journal-title":"Protein Pept. Lett."},{"issue":"13","key":"10.1016\/j.toxicon.2024.107657_bib6","doi-asserted-by":"crossref","first-page":"12316","DOI":"10.1074\/jbc.M413406200","article-title":"Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity\/therapeutic index","volume":"280","author":"Chen","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"19","key":"10.1016\/j.toxicon.2024.107657_bib7","doi-asserted-by":"crossref","first-page":"2309","DOI":"10.4155\/fmc-2018-0170","article-title":"Improving therapeutic potential of antibacterial spider venom peptides: coarse-grain molecular dynamics guided approach","volume":"10","author":"Dubovskii","year":"2018","journal-title":"Future Med. Chem."},{"issue":"3","key":"10.1016\/j.toxicon.2024.107657_bib8","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1007\/s11030-021-10217-3","article-title":"Artificial intelligence to deep learning: machine intelligence approach for drug discovery","volume":"25","author":"Gupta","year":"2021","journal-title":"Mol. Divers."},{"issue":"18","key":"10.1016\/j.toxicon.2024.107657_bib9","doi-asserted-by":"crossref","first-page":"1872","DOI":"10.2174\/156802610793176648","article-title":"Strategies for the discovery and advancement of novel cationic antimicrobial peptides","volume":"10","author":"Hadley","year":"2010","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.toxicon.2024.107657_bib10","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.toxicon.2016.03.014","article-title":"Characterisation of three alpha-helical antimicrobial peptides from the venom of Scorpio maurus palmatus","volume":"117","author":"Harrison","year":"2016","journal-title":"Toxicon"},{"issue":"3","key":"10.1016\/j.toxicon.2024.107657_bib11","doi-asserted-by":"crossref","first-page":"441","DOI":"10.2217\/fmb.15.151","article-title":"Histones as mediators of host defense, inflammation and thrombosis","volume":"11","author":"Hoeksema","year":"2016","journal-title":"Future Microbiol."},{"key":"10.1016\/j.toxicon.2024.107657_bib12","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.biopha.2017.08.011","article-title":"Carapax Trionycis extracts inhibit fibrogenesis of activated hepatic stellate cells via TGF-\u03b21\/Smad and NF\u03baB signaling","volume":"95","author":"Hu","year":"2017","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.toxicon.2024.107657_bib13","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.actbio.2017.04.032","article-title":"Disruption of drug-resistant biofilms using de novo designed short \u03b1-helical antimicrobial peptides with idealized facial amphiphilicity","volume":"57","author":"Khara","year":"2017","journal-title":"Acta Biomater."},{"key":"10.1016\/j.toxicon.2024.107657_bib14","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1146\/annurev-ento-120811-153650","article-title":"Spider-venom peptides: structure, pharmacology, and potential for control of insect pests","volume":"58","author":"King","year":"2013","journal-title":"Annu. Rev. Entomol."},{"issue":"5","key":"10.1016\/j.toxicon.2024.107657_bib15","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1248\/cpb.c18-00079","article-title":"Structural development of cell-penetrating peptides containing cationic proline derivatives","volume":"66","author":"Kobayashi","year":"2018","journal-title":"Chem. Pharmaceut. Bull."},{"issue":"5","key":"10.1016\/j.toxicon.2024.107657_bib16","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/j.toxicon.2006.11.007","article-title":"The universal algorithm of maturation for secretory and excretory protein precursors","volume":"49","author":"Kozlov","year":"2007","journal-title":"Toxicon"},{"issue":"30","key":"10.1016\/j.toxicon.2024.107657_bib17","doi-asserted-by":"crossref","first-page":"20983","DOI":"10.1074\/jbc.M602168200","article-title":"Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity","volume":"281","author":"Kozlov","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/j.toxicon.2024.107657_bib18","doi-asserted-by":"crossref","first-page":"2079","DOI":"10.1074\/jbc.M117.810911","article-title":"Identification of a precursor processing protease from the spider Cupiennius salei essential for venom neurotoxin maturation","volume":"293","author":"Langenegger","year":"2018","journal-title":"J. Biol. Chem."},{"issue":"10","key":"10.1016\/j.toxicon.2024.107657_bib19","doi-asserted-by":"crossref","DOI":"10.3390\/toxins11100611","article-title":"Spider venom: components, modes of action, and novel strategies in transcriptomic and proteomic analyses","volume":"11","author":"Langenegger","year":"2019","journal-title":"Toxins"},{"issue":"1","key":"10.1016\/j.toxicon.2024.107657_bib20","doi-asserted-by":"crossref","first-page":"25","DOI":"10.2174\/1568026615666150703121700","article-title":"Antimicrobial peptide structure and mechanism of action: a focus on the role of membrane structure","volume":"16","author":"Lee","year":"2016","journal-title":"Curr. Top. Med. Chem."},{"issue":"1","key":"10.1016\/j.toxicon.2024.107657_bib21","article-title":"Molecular diversity and evolutionary trends of cysteine-rich peptides from the venom glands of Chinese spider Heteropoda venatoria","volume":"11","author":"Luo","year":"2021","journal-title":"Sci. Rep."},{"issue":"10","key":"10.1016\/j.toxicon.2024.107657_bib22","doi-asserted-by":"crossref","first-page":"2437","DOI":"10.1016\/j.bbamem.2015.07.010","article-title":"Phospholipid-driven differences determine the action of the synthetic antimicrobial peptide OP-145 on Gram-positive bacterial and mammalian membrane model systems","volume":"1848","author":"Malanovic","year":"2015","journal-title":"Biochim. Biophys. Acta Biomembr."},{"issue":"4","key":"10.1016\/j.toxicon.2024.107657_bib23","doi-asserted-by":"crossref","first-page":"1190","DOI":"10.1046\/j.0014-2956.2002.02760.x","article-title":"The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider","volume":"269","author":"Mandard","year":"2002","journal-title":"Eur. J. Biochem."},{"issue":"6","key":"10.1016\/j.toxicon.2024.107657_bib24","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1093\/bbb\/zbab046","article-title":"Characterization of 2 linear peptides without disulfide bridges from the venom of the spider Lycosa poonaensis (Lycosidae)","volume":"85","author":"Megaly","year":"2021","journal-title":"Biosc. Biotech. Biochem."},{"issue":"7","key":"10.1016\/j.toxicon.2024.107657_bib25","doi-asserted-by":"crossref","first-page":"3727","DOI":"10.1007\/s11696-023-02735-1","article-title":"Interaction of antibacterial CM11 peptide with the gram-positive and gram-negative bacterial membrane models: a molecular dynamics simulations study","volume":"77","author":"Mirnejad","year":"2023","journal-title":"Chem. Pap."},{"key":"10.1016\/j.toxicon.2024.107657_bib26","doi-asserted-by":"crossref","DOI":"10.1016\/j.peptides.2021.170594","article-title":"The proline-rich myticalins from Mytilus galloprovincialis display a membrane-permeabilizing antimicrobial mode of action","volume":"143","author":"Pacor","year":"2021","journal-title":"Peptides"},{"issue":"12","key":"10.1016\/j.toxicon.2024.107657_bib27","doi-asserted-by":"crossref","DOI":"10.1007\/s00284-022-03061-7","article-title":"Current treatment strategies against multidrug-resistant bacteria: a review","volume":"79","author":"Parmanik","year":"2022","journal-title":"Curr. Microbiol."},{"issue":"1","key":"10.1016\/j.toxicon.2024.107657_bib28","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/s00726-020-02919-z","article-title":"The introduction of l-phenylalanine into antimicrobial peptide protonectin enhances the selective antibacterial activity of its derivative phe-Prt against Gram-positive bacteria","volume":"53","author":"Peng","year":"2021","journal-title":"Amino Acids"},{"issue":"11","key":"10.1016\/j.toxicon.2024.107657_bib29","doi-asserted-by":"crossref","first-page":"7570","DOI":"10.1021\/acs.jmedchem.3c00460","article-title":"To Fold or not to fold: diastereomeric optimization of an \u03b1-helical antimicrobial peptide","volume":"66","author":"Personne","year":"2023","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.toxicon.2024.107657_bib30","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2019.02866","article-title":"Mechanisms of action for antimicrobial peptides with antibacterial and antibiofilm functions","volume":"10","author":"Raheem","year":"2019","journal-title":"Front. Microbiol."},{"issue":"1","key":"10.1016\/j.toxicon.2024.107657_bib31","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.drudis.2020.10.002","article-title":"Deep learning in next-generation sequencing","volume":"26","author":"Schmidt","year":"2020","journal-title":"Drug Discov. Today"},{"issue":"12","key":"10.1016\/j.toxicon.2024.107657_bib32","doi-asserted-by":"crossref","DOI":"10.3390\/toxins10120522","article-title":"Loxosceles gaucho spider venom: an untapped source of antimicrobial agents","volume":"10","author":"Segura-Ram\u00edrez","year":"2018","journal-title":"Toxins"},{"issue":"11","key":"10.1016\/j.toxicon.2024.107657_bib33","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1093\/abbs\/gmaa107","article-title":"Molecular diversification of antimicrobial peptides from the wolf spider Lycosa sinensisvenom based on peptidomic, transcriptomic, and bioinformatic analyses","volume":"52","author":"Tang","year":"2020","journal-title":"Acta Biochim. Biophys. Sin."},{"issue":"7","key":"10.1016\/j.toxicon.2024.107657_bib34","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1038\/s41587-021-01156-3","article-title":"SignalP 6.0 predicts all five types of signal peptides using protein language models","volume":"40","author":"Teufel","year":"2022","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.toxicon.2024.107657_bib35","doi-asserted-by":"crossref","DOI":"10.3389\/fphar.2021.640938","article-title":"Editorial: natural antimicrobial peptides: hope for new antibiotic lead molecules","volume":"12","author":"Uddin","year":"2021","journal-title":"Front. Pharmacol."},{"issue":"6","key":"10.1016\/j.toxicon.2024.107657_bib36","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1002\/1873-3468.13705","article-title":"Curved or linear? Predicting the 3-dimensional structure of \u03b1-helical antimicrobial peptides in an amphipathic environment","volume":"594","author":"Van den Bergen","year":"2020","journal-title":"FEBS Lett."},{"issue":"13","key":"10.1016\/j.toxicon.2024.107657_bib37","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1134\/S0006297909130069","article-title":"Molecular diversity of spider venom","volume":"74","author":"Vassilevski","year":"2009","journal-title":"Biochemistry-Moscow"},{"key":"10.1016\/j.toxicon.2024.107657_bib38","doi-asserted-by":"crossref","DOI":"10.1016\/j.addr.2021.05.028","article-title":"Antimicrobial peptides towards clinical application: delivery and formulation","volume":"175","author":"Wang","year":"2021","journal-title":"Adv. Drug Deliv. Rev."},{"issue":"5","key":"10.1016\/j.toxicon.2024.107657_bib39","doi-asserted-by":"crossref","DOI":"10.3390\/toxins8050119","article-title":"The spider venom peptide lycosin-II has potent antimicrobial activity against clinically isolated bacteria","volume":"8","author":"Wang","year":"2016","journal-title":"Toxins"},{"issue":"2","key":"10.1016\/j.toxicon.2024.107657_bib40","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1038\/nprot.2007.521","article-title":"Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances","volume":"3","author":"Wiegand","year":"2008","journal-title":"Nat. Protoc."},{"issue":"25","key":"10.1016\/j.toxicon.2024.107657_bib41","doi-asserted-by":"crossref","first-page":"8102","DOI":"10.1021\/bi9904104","article-title":"Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides","volume":"38","author":"Zhang","year":"1999","journal-title":"Biochemistry"},{"issue":"44","key":"10.1016\/j.toxicon.2024.107657_bib42","doi-asserted-by":"crossref","first-page":"9379","DOI":"10.1039\/C7OB02233F","article-title":"Arginine modification of lycosin-I to improve inhibitory activity against cancer cells","volume":"15","author":"Zhang","year":"2017","journal-title":"Org. Biomol. Chem."}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010124002290?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010124002290?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,22]],"date-time":"2025-09-22T21:24:29Z","timestamp":1758576269000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010124002290"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4]]},"references-count":42,"alternative-id":["S0041010124002290"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2024.107657","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2024,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Characterization of an antimicrobial peptide family from the venom gland of Heteropoda venatoria","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2024.107657","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"107657"}}