{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T01:23:14Z","timestamp":1760145794091,"version":"build-2065373602"},"reference-count":53,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2024,8,21]],"date-time":"2024-08-21T00:00:00Z","timestamp":1724198400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004543","name":"China Scholarship Council","doi-asserted-by":"publisher","award":["202003250087"],"award-info":[{"award-number":["202003250087"]}],"id":[{"id":"10.13039\/501100004543","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Worldwide, it is estimated that there are 1.8 to 2.7 million cases of envenoming caused by snakebites. Snake venom is a complex mixture of protein toxins, lipids, small molecules, and salts, with the proteins typically responsible for causing pathology in snakebite victims. For their chemical characterization and identification, analytical methods are required. Reversed-phase liquid chromatography coupled with electrospray ionization mass spectrometry (RP-LC-ESI-MS) is a widely used technique due to its ease of use, sensitivity, and ability to be directly coupled after LC separation. This method allows for the efficient separation of complex mixtures and sensitive detection of analytes. On the other hand, matrix-assisted laser desorption\/ionization mass spectrometry (MALDI-MS) is also sometimes used, and though it typically requires additional sample preparation steps, it offers desirable suitability for the analysis of larger biomolecules. In this study, seven medically important viperid snake venoms were separated into their respective venom toxins and measured by ESI-MS. In parallel, using nanofractionation analytics, post-column high-resolution fractionation was used to collect the eluting toxins for further processing for MALDI-MS analysis. Our comparative results showed that the deconvoluted snake venom toxin masses were observed with good sensitivity from both ESI-MS and MALDI-MS approaches and presented overlap in the toxin masses recovered (between 25% and 57%, depending on the venom analyzed). The mass range of the toxins detected in high abundance was between 4 and 28 kDa. In total, 39 masses were found in both the ESI-MS and\/or MALDI-MS analyses, with most being between 5 and 9 kDa (46%), 13 and 15 kDa (38%), and 24 and 28 kDa (13%) in size. Next to the post-column MS analyses, additional coagulation bioassaying was performed to demonstrate the parallel post-column assessment of venom activity in the workflow. Most nanofractionated venoms exhibited anticoagulant activity, with three venoms additionally exhibiting toxins with clear procoagulant activity (Bothrops asper, Crotalus atrox, and Daboia russelii) observed post-column. The results of this study highlight the complementarity of ESI-MS and MALDI-MS approaches for characterizing snake venom toxins and provide a complementary overview of defined toxin masses found in a diversity of viper snake venoms.<\/jats:p>","DOI":"10.3390\/toxins16080370","type":"journal-article","created":{"date-parts":[[2024,8,22]],"date-time":"2024-08-22T06:28:51Z","timestamp":1724308131000},"page":"370","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Nanofractionation Analytics for Comparing MALDI-MS and ESI-MS Data of Viperidae Snake Venom Toxins"],"prefix":"10.3390","volume":"16","author":[{"given":"Haifeng","family":"Xu","sequence":"first","affiliation":[{"name":"Department of Chemistry and Pharmaceutical Sciences, Division of BioAnalytical Chemistry, Faculty of Science, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands"},{"name":"Centre for Analytical Sciences Amsterdam (CASA), 1012 WX Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jesse","family":"Mastenbroek","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Pharmaceutical Sciences, Division of BioAnalytical Chemistry, Faculty of Science, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Natascha T. B.","family":"Krikke","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Pharmaceutical Sciences, Division of BioAnalytical Chemistry, Faculty of Science, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0007-4844-8073","authenticated-orcid":false,"given":"Susan","family":"El-Asal","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Pharmaceutical Sciences, Division of BioAnalytical Chemistry, Faculty of Science, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rama","family":"Mutlaq","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Pharmaceutical Sciences, Division of BioAnalytical Chemistry, Faculty of Science, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8035-4719","authenticated-orcid":false,"given":"Nicholas R.","family":"Casewell","sequence":"additional","affiliation":[{"name":"Centre for Snakebite Research & Interventions, Liverpool School of Tropical Medicine, Liverpool L3 5QA, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2929-1086","authenticated-orcid":false,"given":"Julien","family":"Slagboom","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Pharmaceutical Sciences, Division of BioAnalytical Chemistry, Faculty of Science, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands"},{"name":"Centre for Analytical Sciences Amsterdam (CASA), 1012 WX Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0011-5612","authenticated-orcid":false,"given":"Jeroen","family":"Kool","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Pharmaceutical Sciences, Division of BioAnalytical Chemistry, Faculty of Science, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands"},{"name":"Centre for Analytical Sciences Amsterdam (CASA), 1012 WX Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2024,8,21]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Kasturiratne, A., Wickremasinghe, A.R., De Silva, N., Gunawardena, N.K., Pathmeswaran, A., Premaratna, R., Savioli, L., Lalloo, D.G., and De Silva, H.J. (2008). The global burden of snakebite: A literature analysis and modelling based on regional estimates of envenoming and deaths. PLoS Med., 5.","DOI":"10.1371\/journal.pmed.0050218"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Williams, D.J., Faiz, M.A., Abela-Ridder, B., Ainsworth, S., Bulfone, T.C., Nickerson, A.D., Habib, A.G., Junghanss, T., Fan, H.W., and Turner, M. (2019). Strategy for a globally coordinated response to a priority neglected tropical disease: Snakebite envenoming. PLoS Negl. Trop. Dis., 13.","DOI":"10.1371\/journal.pntd.0007059"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"17063","DOI":"10.1038\/nrdp.2017.63","article-title":"Snakebite envenoming","volume":"3","author":"Calvete","year":"2017","journal-title":"Nat. Rev. Dis. Primers"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2175","DOI":"10.1016\/S0140-6736(19)31232-2","article-title":"Snakebite\u2014Emerging from the shadows of neglect","volume":"393","author":"Lancet","year":"2019","journal-title":"Lancet"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1111\/bjh.14591","article-title":"Haemotoxic snake venoms: Their functional activity, impact on snakebite victims and pharmaceutical promise","volume":"177","author":"Slagboom","year":"2017","journal-title":"Br. J. Haematol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1874","DOI":"10.2174\/0929867324666170605091546","article-title":"Snake Venom: From Deadly Toxins to Life-saving Therapeutics","volume":"24","author":"Waheed","year":"2017","journal-title":"Curr. Med. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Sanhajariya, S., Duffull, S.B., and Isbister, G.K. (2018). Pharmacokinetics of Snake Venom. Toxins, 10.","DOI":"10.3390\/toxins10020073"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Tasoulis, T., and Isbister, G.K. (2017). A Review and Database of Snake Venom Proteomes. Toxins, 9.","DOI":"10.3390\/toxins9090290"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1111\/j.1538-7836.2011.04279.x","article-title":"Toxins in thrombosis and haemostasis: Potential beyond imagination","volume":"9","author":"Kini","year":"2011","journal-title":"J. Thromb. Haemost."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1159\/000092424","article-title":"Serine proteases affecting blood coagulation and fibrinolysis from snake venoms","volume":"34","author":"Kini","year":"2006","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Guti\u00e9rrez, J.M., Escalante, T., Rucavado, A., and Herrera, C. (2016). Hemorrhage Caused by Snake Venom Metalloproteinases: A Journey of Discovery and Understanding. Toxins, 8.","DOI":"10.3390\/toxins8040093"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Preciado, L.M., Perea\u00f1ez, J.A., and Comer, J. (2019). Potential of Matrix Metalloproteinase Inhibitors for the Treatment of Local Tissue Damage Induced by a Type P-I Snake Venom Metalloproteinase. Toxins, 12.","DOI":"10.3390\/toxins12010008"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/S0300-9084(00)01163-9","article-title":"Snake venom metalloproteinases: Their role in the pathogenesis of local tissue damage","volume":"82","author":"Rucavado","year":"2000","journal-title":"Biochimie"},{"key":"ref_14","unstructured":"Sunagar, K., Jackson, T.N.W., Reeks, T., and Fry, B.G. (2015). Group I phospholipase A2 enzymes. Venomous Reptiles and Their Toxins: Evolution, Pathophysiology and Biodiscovery, Oxford University Press."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Xiao, H., Pan, H., Liao, K., Yang, M., and Huang, C. (2017). Snake Venom PLA2, a Promising Target for Broad-Spectrum Antivenom Drug Development. BioMed Res. Int., 2017.","DOI":"10.1155\/2017\/6592820"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"107187","DOI":"10.1016\/j.microc.2022.107187","article-title":"Analytical strategies in venomics","volume":"175","author":"Slagboom","year":"2022","journal-title":"Microchem. J."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"2594","DOI":"10.1002\/elps.201500207","article-title":"Fractionation and proteomic analysis of the Walterinnesia aegyptia snake venom using OFFGEL and MALDI-TOF-MS techniques","volume":"36","author":"Combemale","year":"2015","journal-title":"Electrophoresis"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1016\/j.toxicon.2007.12.017","article-title":"Partial purification of cytolytic venom proteins from the box jellyfish, Chironex fleckeri","volume":"51","author":"Brinkman","year":"2008","journal-title":"Toxicon"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.toxicon.2013.02.006","article-title":"Isolation, characterization, cloning and expression of an alpha-neurotoxin from the venom of the Mexican coral snake Micrurus laticollaris (Squamata: Elapidae)","volume":"66","author":"Smith","year":"2013","journal-title":"Toxicon"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/S0041-0101(00)00165-3","article-title":"Partial characterization of a basic protein from Crotalus molossus molossus (northern blacktail rattlesnake) venom and production of a monoclonal antibody","volume":"39","author":"Soliz","year":"2001","journal-title":"Toxicon"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Slagboom, J., Mladi\u0107, M., Xie, C., Kazandjian, T.D., Vonk, F., Somsen, G.W., Casewell, N.R., and Kool, J. (2020). High throughput screening and identification of coagulopathic snake venom proteins and peptides using nanofractionation and proteomics approaches. PLoS Negl. Trop. Dis., 14.","DOI":"10.1371\/journal.pntd.0007802"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Xie, C., Albulescu, L.-O., Still, K.B.M., Slagboom, J., Zhao, Y., Jiang, Z., Somsen, G.W., Vonk, F.J., Casewell, N.R., and Kool, J. (2020). Varespladib inhibits the phospholipase A2 and coagulopathic activities of venom components from hemotoxic snakes. Biomedicines, 8.","DOI":"10.3390\/biomedicines8060165"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"5987","DOI":"10.1007\/s00216-017-0531-3","article-title":"Rapid screening and identification of ACE inhibitors in snake venoms using at-line nanofractionation LC-MS","volume":"409","author":"Mladic","year":"2017","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Xie, C., Bittenbinder, M.A., Slagboom, J., Arrahman, A., Bruijns, S., Somsen, G.W., Vonk, F.J., Casewell, N.R., Garc\u00eda-Vallejo, J.J., and Kool, J. (2021). Erythrocyte haemotoxicity profiling of snake venom toxins after nanofractionation. J. Chromatogr. B Anal. Technol. Biomed. Life Sci., 1176.","DOI":"10.1016\/j.jchromb.2021.122586"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Bittenbinder, M.A., Capinha, L., Pereira, D.D.C., Slagboom, J., van de Velde, B., Casewell, N.R., Jennings, P., Kool, J., and Vonk, F.J. (2023). Development of a high-throughput in vitro screening method for the assessment of cell-damaging activities of snake venoms. PLoS Negl. Trop. Dis., 17.","DOI":"10.1371\/journal.pntd.0011564"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Bickler, P.E. (2020). Amplification of Snake Venom Toxicity by Endogenous Signaling Pathways. Toxins, 12.","DOI":"10.3390\/toxins12020068"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1038\/nature10607","article-title":"A heteromeric Texas coral snake toxin targets acid-sensing ion channels to produce pain","volume":"479","author":"Bohlen","year":"2011","journal-title":"Nature"},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Suntravat, M., Sanchez, O., Reyes, A., Cirilo, A., Ocheltree, J.S., Galan, J.A., Salazar, E., Davies, P., and Sanchez, E.E. (2021). Evaluation of signaling pathways profiling in human dermal endothelial cells treated by snake venom cysteine-rich secretory proteins (Svcrisps) from north american snakes using reverse phase protein array (rppa). Toxins, 13.","DOI":"10.3390\/toxins13090613"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.jprot.2009.01.008","article-title":"Snake venomics and antivenomics: Proteomic tools in the design and control of antivenoms for the treatment of snakebite envenoming","volume":"72","author":"Lomonte","year":"2009","journal-title":"J. Proteom."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2047","DOI":"10.1002\/rcm.1148","article-title":"Analysis of Colubroidea snake venoms by liquid chromatography with mass spectrometry: Evolutionary and toxinological implications","volume":"17","author":"Fry","year":"2003","journal-title":"Rapid Commun. Mass Spectrom."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2539","DOI":"10.1021\/acs.jproteome.5b00305","article-title":"Venom proteomics of indonesian king cobra, ophiophagus hannah: Integrating top-down and bottom-up approaches","volume":"14","author":"Petras","year":"2015","journal-title":"J. Proteome Res."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Valente, R.H., Nicolau, C.A., Perales, J., and Neves-Ferreira, A.G. (2016). Snake Venom Proteopeptidomics: What Lies Behind the Curtain. Venom Genomics and Proteomics, Springer.","DOI":"10.1007\/978-94-007-6416-3_6"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"M111.009407","DOI":"10.1074\/mcp.M111.009407","article-title":"Principles of electrospray ionization","volume":"10","author":"Wilm","year":"2011","journal-title":"Mol. Cell. Proteom."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Xie, C., Albulescu, L.-O., Bittenbinder, M.A., Somsen, G.W., Vonk, F.J., Casewell, N.R., and Kool, J. (2020). Neutralizing effects of small molecule inhibitors and metal chelators on coagulopathic Viperinae snake venom toxins. Biomedicines, 8.","DOI":"10.1101\/2020.06.02.129643"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.nbt.2017.05.005","article-title":"Guiding recombinant antivenom development by omics technologies","volume":"45","author":"Laustsen","year":"2018","journal-title":"New Biotechnol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"20651","DOI":"10.1073\/pnas.1314702110","article-title":"The king cobra genome reveals dynamic gene evolution and adaptation in the snake venom system","volume":"110","author":"Vonk","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.toxicon.2012.09.008","article-title":"Non-enzymatic proteins from snake venoms: A gold mine of pharmacological tools and drug leads","volume":"62","author":"McCleary","year":"2013","journal-title":"Toxicon"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Boldrini-Fran\u00e7a, J., Pinheiro-Junior, E.L., Peigneur, S., Pucca, M.B., Cerni, F.A., Borges, R.J., Costa, T.R., Carone, S.E.I., Fontes, M.R.d.M., and Sampaio, S.V. (2020). Beyond hemostasis: A snake venom serine protease with potassium channel blocking and potential antitumor activities. Sci. Rep., 10.","DOI":"10.1038\/s41598-020-61258-x"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/j.jprot.2008.10.003","article-title":"Combined snake venomics and venom gland transcriptomic analysis of the ocellated carpet viper, Echis ocellatus","volume":"71","author":"Wagstaff","year":"2009","journal-title":"J. Proteom."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1016\/j.toxicon.2009.06.011","article-title":"Studies on the venom proteome of Bothrops asper: Perspectives and applications","volume":"54","author":"Sanz","year":"2009","journal-title":"Toxicon"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"3055","DOI":"10.1021\/pr900249q","article-title":"Exploring the venom proteome of the western diamondback rattlesnake, Crotalus atrox, via snake venomics and combinatorial peptide ligand library approaches","volume":"8","author":"Calvete","year":"2009","journal-title":"J. Proteome Res."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/j.toxicon.2015.06.027","article-title":"Unveiling the complexities of Daboia russelii venom, a medically important snake of India, by tandem mass spectrometry","volume":"107","author":"Sharma","year":"2015","journal-title":"Toxicon"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Dingwoke, E.J., Adamude, F.A., Mohamed, G., Klein, A., Salihu, A., Abubakar, M.S., and Sallau, A.B. (2021). Venom proteomic analysis of medically important Nigerian viper Echis ocellatus and Bitis arietans snake species. Biochem. Biophys. Rep., 28.","DOI":"10.1016\/j.bbrep.2021.101164"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.jprot.2016.02.030","article-title":"Proteomic identification of gender molecular markers in Bothrops jararaca venom","volume":"139","author":"Zelanis","year":"2016","journal-title":"J. Proteom."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Patra, A., Kalita, B., Chanda, A., and Mukherjee, A.K. (2017). Proteomics and antivenomics of Echis carinatus carinatus venom: Correlation with pharmacological properties and pathophysiology of envenomation. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-17227-y"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Damm, M., Hempel, B.-F., and S\u00fcssmuth, R.D. (2021). Old world vipers-a review about snake venom proteomics of viperinae and their variations. Toxins, 13.","DOI":"10.3390\/toxins13060427"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.toxicon.2011.01.006","article-title":"Haemostatically active proteins in snake venoms","volume":"57","author":"Sajevic","year":"2011","journal-title":"Toxicon"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0009-3084(03)00097-5","article-title":"Analysis of the lipid composition of bull spermatozoa by MALDI-TOF mass spectrometry\u2014A cautionary note","volume":"126","author":"Schiller","year":"2003","journal-title":"Phys. Lipids"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1002\/rcm.2853","article-title":"The venom of the snake genus Atheris contains a new class of peptides with clusters of histidine and glycine residues","volume":"21","author":"Favreau","year":"2007","journal-title":"Rapid Commun. Mass Spectrom."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1703","DOI":"10.1002\/rcm.1973","article-title":"Fast analysis of low molecular mass compounds present in snake venom: Identification of ten new pyroglutamate-containing peptides","volume":"19","author":"Wermelinger","year":"2005","journal-title":"Rapid Commun. Mass Spectrom."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"3467","DOI":"10.1002\/rcm.3240","article-title":"Mass fingerprinting of toxic fractions from the venom of the Indian red scorpion, Mesobuthus tamulus: Biotope-specific variation in the expression of venom peptides","volume":"21","author":"Newton","year":"2007","journal-title":"Rapid Commun. Mass Spectrom."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1016\/j.toxicon.2008.03.029","article-title":"Mass spectrometry analysis, amino acid sequence and biological activity of venom components from the Brazilian scorpion Opisthacanthus cayaporum","volume":"51","author":"Schwartz","year":"2008","journal-title":"Toxicon"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.ijms.2009.12.015","article-title":"Comparison of MALDI-TOF\/MS and LC-QTOF\/MS methods for the identification of enteric bacteria","volume":"291","author":"Mott","year":"2010","journal-title":"Int. J. Mass Spectrom."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/16\/8\/370\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T15:40:28Z","timestamp":1760110828000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/16\/8\/370"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,8,21]]},"references-count":53,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2024,8]]}},"alternative-id":["toxins16080370"],"URL":"https:\/\/doi.org\/10.3390\/toxins16080370","relation":{},"ISSN":["2072-6651"],"issn-type":[{"type":"electronic","value":"2072-6651"}],"subject":[],"published":{"date-parts":[[2024,8,21]]}}}