{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T02:06:38Z","timestamp":1793066798694,"version":"4.5.0"},"reference-count":56,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,1,28]],"date-time":"2025-01-28T00:00:00Z","timestamp":1738022400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","award":["001"],"award-info":[{"award-number":["001"]}],"id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005942","name":"Butantan Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005942","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Chromatography A"],"published-print":{"date-parts":[[2025,2]]},"DOI":"10.1016\/j.chroma.2025.465715","type":"journal-article","created":{"date-parts":[[2025,1,22]],"date-time":"2025-01-22T07:50:35Z","timestamp":1737532235000},"page":"465715","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"special_numbering":"C","title":["Hydrophilic interaction chromatography coupled to high resolution mass spectrometry (HILIC-LC-HRMS): An approach to study natural peptides in Viperidae snake venom"],"prefix":"10.1016","volume":"1743","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6486-337X","authenticated-orcid":false,"given":"Monica V.","family":"Falla","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6978-442X","authenticated-orcid":false,"given":"Ivo","family":"Lebrun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcos A.","family":"Pudenzi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laudiceia A.","family":"Oliveira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heloisa F.","family":"Almeida","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathalia G.","family":"Santos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariana S.","family":"Rodrigues","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick J.","family":"Spencer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marisa M.","family":"Rocha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2406-0860","authenticated-orcid":false,"given":"Daniel C.","family":"Pimenta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9633-7219","authenticated-orcid":false,"given":"Guilherme R.","family":"Coelho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.chroma.2025.465715_bib0001","doi-asserted-by":"crossref","first-page":"851","DOI":"10.3390\/toxins13120851","article-title":"Neglected venomous animals and toxins: underrated biotechnological tools in drug development","volume":"13","author":"Coelho","year":"2021","journal-title":"Toxins. (Basel)"},{"key":"10.1016\/j.chroma.2025.465715_bib0002","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":"Guti\u00e9rrez","year":"2009","journal-title":"J. Proteomics."},{"key":"10.1016\/j.chroma.2025.465715_bib0003","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1002\/jms.1242","article-title":"Snake venomics. Strategy and applications","author":"Calvete","year":"2007","journal-title":"J. Mass Spectrometry"},{"key":"10.1016\/j.chroma.2025.465715_bib0004","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1111\/j.1476-5381.1965.tb02091.x","article-title":"A bradykinin-potentiating factor (BPF) present in the venom of Bothrops jararaca","volume":"24","author":"FERREIRA","year":"1965","journal-title":"Br. J. Pharmacol. ChemOther"},{"key":"10.1016\/j.chroma.2025.465715_bib0005","doi-asserted-by":"crossref","first-page":"2278","DOI":"10.1021\/pr901027r","article-title":"Analysis of the ontogenetic variation in the venom proteome\/peptidome of bothrops jararaca reveals different strategies to deal with prey","volume":"9","author":"Zelanis","year":"2010","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.chroma.2025.465715_bib0006","doi-asserted-by":"crossref","first-page":"1288","DOI":"10.1016\/j.toxicon.2008.02.019","article-title":"High throughput screening of bradykinin-potentiating peptides in Bothrops moojeni snake venom using precursor ion mass spectrometry","volume":"51","author":"Menin","year":"2008","journal-title":"Toxicon."},{"key":"10.1016\/j.chroma.2025.465715_bib0007","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 Spectrometry"},{"key":"10.1016\/j.chroma.2025.465715_bib0008","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.jprot.2016.06.029","article-title":"An in-depth snake venom proteopeptidome characterization: Benchmarking Bothrops jararaca","volume":"151","author":"Nicolau","year":"2017","journal-title":"J. Proteomics."},{"key":"10.1016\/j.chroma.2025.465715_bib0009","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/j.peptides.2004.04.006","article-title":"Identification of five new bradykinin potentiating peptides (BPPs) from Bothrops jararaca crude venom by using electrospray ionization tandem mass spectrometry after a two-step liquid chromatography","volume":"25","author":"Ianzer","year":"2004","journal-title":"Peptides (N.Y.)"},{"key":"10.1016\/j.chroma.2025.465715_bib0010","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.1016\/j.bbrc.2005.10.130","article-title":"Identification and functional analysis of a novel bradykinin inhibitory peptide in the venoms of New World Crotalinae pit vipers","volume":"338","author":"James Graham","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.chroma.2025.465715_bib0011","doi-asserted-by":"crossref","first-page":"1180","DOI":"10.1016\/j.bbagen.2015.02.005","article-title":"New proline-rich oligopeptides from the venom of African adders: Insights into the hypotensive effect of the venoms","volume":"1850","author":"Kodama","year":"2015","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.chroma.2025.465715_bib0012","doi-asserted-by":"crossref","first-page":"2778","DOI":"10.3390\/molecules24152778","article-title":"Hypotensive Snake Venom Components\u2014A Mini-Review","volume":"24","author":"P\u00e9terfi","year":"2019","journal-title":"Molecules."},{"key":"10.1016\/j.chroma.2025.465715_bib0013","first-page":"424","article-title":"Self-proteolysis regulation in the Bothrops jararaca venom: The metallopeptidases and their intrinsic peptidic inhibitor","volume":"147","author":"Marques-Porto","year":"2008","journal-title":"Compar. Biochem. Physiol. Part C"},{"key":"10.1016\/j.chroma.2025.465715_bib0014","doi-asserted-by":"crossref","first-page":"474","DOI":"10.3390\/toxins10110474","article-title":"Snake venom peptides: tools of biodiscovery","volume":"10","author":"Munawar","year":"2018","journal-title":"Toxins. (Basel)"},{"key":"10.1016\/j.chroma.2025.465715_bib0015","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1074\/mcp.M112.019331","article-title":"Peptidomics of three bothrops snake venoms: Insights into the molecular diversification of proteomes and peptidomes","volume":"11","author":"Tashima","year":"2012","journal-title":"Mol. Cellular Proteomics"},{"key":"10.1016\/j.chroma.2025.465715_bib0016","series-title":"An Integrated View of the Molecular Recognition and Toxinology - From Analytical Procedures to Biomedical Applications","article-title":"Peptidomic Analysis of Animal Venoms","author":"Cunha","year":"2013"},{"key":"10.1016\/j.chroma.2025.465715_bib0017","first-page":"14","article-title":"Snake Venomics: Fundamentals, Recent Updates, and a Look to the Next Decade","author":"Tan","year":"2022","journal-title":"Toxins. (Basel)"},{"key":"10.1016\/j.chroma.2025.465715_bib0018","doi-asserted-by":"crossref","first-page":"1736","DOI":"10.1016\/j.febslet.2009.03.029","article-title":"Venoms, venomics, antivenomics","volume":"583","author":"Calvete","year":"2009","journal-title":"FEBS Lett."},{"key":"10.1016\/j.chroma.2025.465715_bib0019","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1586\/epr.11.61","article-title":"Proteomic tools against the neglected pathology of snake bite envenoming","volume":"8","author":"Calvete","year":"2014","journal-title":"Expert. Rev. Proteomics."},{"key":"10.1016\/j.chroma.2025.465715_bib0020","doi-asserted-by":"crossref","first-page":"316","DOI":"10.2174\/1573412916666200402101501","article-title":"Hydrophilic Interaction Liquid Chromatography (HILIC): latest applications in the pharmaceutical researches","volume":"17","author":"Erkmen","year":"2021","journal-title":"Curr. Pharm. Anal."},{"key":"10.1016\/j.chroma.2025.465715_bib0021","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1002\/jssc.200900742","article-title":"HILIC methods in pharmaceutical analysis","volume":"33","author":"Dejaegher","year":"2010","journal-title":"J. Sep. Sci."},{"key":"10.1016\/j.chroma.2025.465715_bib0022","doi-asserted-by":"crossref","first-page":"1784","DOI":"10.1002\/jssc.200600199","article-title":"Hydrophilic interaction chromatography","volume":"29","author":"Hemstr\u00f6m","year":"2006","journal-title":"J. Sep. Sci."},{"key":"10.1016\/j.chroma.2025.465715_bib0023","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.jchromb.2003.08.026","article-title":"Bioanalytical liquid chromatography tandem mass spectrometry methods on underivatized silica columns with aqueous\/organic mobile phases","volume":"796","author":"Naidong","year":"2003","journal-title":"J. Chromatogr. B Analyt. Technol. Biomed. Life Sci."},{"key":"10.1016\/j.chroma.2025.465715_bib0024","first-page":"1613","article-title":"A clean-up strategy for identification of circulating endogenous short peptides in human plasma by zwitterionic hydrophilic liquid chromatography and untargeted peptidomics identification","author":"Piovesana","year":"2020","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.chroma.2025.465715_bib0025","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.jbbm.2004.01.006","article-title":"Peptide separation by hydrophilic-interaction chromatography: a review","volume":"60","author":"Yoshida","year":"2004","journal-title":"J. Biochem. Biophys. Methods"},{"key":"10.1016\/j.chroma.2025.465715_bib0026","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1016\/j.foodchem.2014.10.104","article-title":"Improved short peptide identification using HILIC-MS\/MS: Retention time prediction model based on the impact of amino acid position in the peptide sequence","volume":"173","author":"Le Maux","year":"2015","journal-title":"Food Chem."},{"key":"10.1016\/j.chroma.2025.465715_bib0027","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1007\/s00216-008-1865-7","article-title":"Hydrophilic interaction liquid chromatography (HILIC) in proteomics","volume":"391","author":"Boersema","year":"2008","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.chroma.2025.465715_bib0028","doi-asserted-by":"crossref","first-page":"3395","DOI":"10.1007\/s00216-019-01815-0","article-title":"Identification of bioactive short peptides in cow milk by high-performance liquid chromatography on C18 and porous graphitic carbon coupled to high-resolution mass spectrometry","volume":"411","author":"Montone","year":"2019","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.chroma.2025.465715_bib0029","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1002\/jssc.201400969","article-title":"Applications of hydrophilic interaction chromatography to amino acids, peptides, and proteins","volume":"38","author":"Periat","year":"2015","journal-title":"J. Sep. Sci."},{"key":"10.1016\/j.chroma.2025.465715_bib0030","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1021\/acsptsci.9b00079","article-title":"Venom peptides with dual modulatory activity on the voltage-gated sodium channel Na V 1.1 provide novel leads for development of antiepileptic drugs","volume":"3","author":"Chow","year":"2019","journal-title":"ACS. Pharmacol. Transl. Sci."},{"key":"10.1016\/j.chroma.2025.465715_bib0031","doi-asserted-by":"crossref","first-page":"4511","DOI":"10.3390\/molecules25194511","article-title":"Two new indole alkaloids from toad venom of Bufo bufo gargarizans","volume":"25","author":"Chen","year":"2020","journal-title":"Molecules."},{"key":"10.1016\/j.chroma.2025.465715_bib0032","doi-asserted-by":"crossref","first-page":"3076","DOI":"10.1002\/pmic.201200224","article-title":"Short-chain peptides identification of scorpion Buthus martensi Karsch venom by employing high orthogonal 2D-HPLC system and tandem mass spectrometry","volume":"12","author":"Xu","year":"2012","journal-title":"Proteomics"},{"key":"10.1016\/j.chroma.2025.465715_bib0033","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":"10.1016\/j.chroma.2025.465715_bib0034","doi-asserted-by":"crossref","first-page":"5751","DOI":"10.1007\/s00216-018-1253-x","article-title":"Liquid chromatographic nanofractionation with parallel mass spectrometric detection for the screening of plasmin inhibitors and (metallo)proteinases in snake venoms","volume":"410","author":"Zietek","year":"2018","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.chroma.2025.465715_bib0035","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.toxicon.2021.03.014","article-title":"Proteomic analysis of three medically important Nigerian Naja (Naja haje, Naja katiensis and Naja nigricollis) snake venoms","volume":"197","author":"Adamude","year":"2021","journal-title":"Toxicon."},{"key":"10.1016\/j.chroma.2025.465715_bib0036","first-page":"10","article-title":"Organic and peptidyl constituents of snake venoms: The picture is vastly more complex than we imagined","author":"Villar-Briones","year":"2018","journal-title":"Toxins. (Basel)"},{"key":"10.1016\/j.chroma.2025.465715_bib0037","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.chroma.2025.465715_bib0038","doi-asserted-by":"crossref","first-page":"1940","DOI":"10.1016\/j.peptides.2009.06.035","article-title":"Codon number shapes peptide redundancy in the universal proteome composition","volume":"30","author":"Kusalik","year":"2009","journal-title":"Peptides (N.Y.)"},{"key":"10.1016\/j.chroma.2025.465715_bib0039","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1093\/molbev\/msh091","article-title":"Assembling an arsenal: origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences","volume":"21","author":"Fry","year":"2004","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.chroma.2025.465715_bib0040","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1021\/acs.jnatprod.3c00991","article-title":"Structural characterization and rat aortic vascular reactivity of bradykinin-potentiating peptides (BPPs) from the snake venom of Bothrops moojeni from Delta do Parna\u00edba Region, Brazil","volume":"87","author":"Costa","year":"2024","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.chroma.2025.465715_bib0041","doi-asserted-by":"crossref","first-page":"1635","DOI":"10.1007\/s00726-021-03055-y","article-title":"Antimicrobial peptidomes of Bothrops atrox and Bothrops jararacussu snake venoms","volume":"53","author":"da Silva Caldeira","year":"2021","journal-title":"Amino Acids."},{"key":"10.1016\/j.chroma.2025.465715_bib0042","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":"10.1016\/j.chroma.2025.465715_bib0043","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.jprot.2013.10.036","article-title":"Venomics of new world pit vipers: Genus-wide comparisons of venom proteomes across agkistrodon","volume":"96","author":"Lomonte","year":"2014","journal-title":"J. Proteomics."},{"key":"10.1016\/j.chroma.2025.465715_bib0044","article-title":"Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros","volume":"23","author":"Fucase","year":"2017","journal-title":"J. Venomous Anim. Toxins Including Trop. Dis."},{"key":"10.1016\/j.chroma.2025.465715_bib0045","doi-asserted-by":"crossref","unstructured":"N. Murayama, M.A.F. Hayashi, H. Ohi, L.A.F. Ferreira, V. V Hermann, H. Saito, Y. Fujita, S. Higuchi, B.L. Fernandes, T. Yamane, A.C.M. De Camargo, Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a precursor of seven bradykinin-potentiating peptides and a C-type natriuretic peptide, 1997. www.pnas.org.","DOI":"10.1073\/pnas.94.4.1189"},{"key":"10.1016\/j.chroma.2025.465715_bib0046","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 Spectrometry"},{"key":"10.1016\/j.chroma.2025.465715_bib0047","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1016\/j.bbrc.2007.11.027","article-title":"Molecular characterisation of endogenous snake venom metalloproteinase inhibitors","volume":"365","author":"Wagstaff","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.chroma.2025.465715_bib0048","doi-asserted-by":"crossref","first-page":"1034","DOI":"10.1002\/rcm.2931","article-title":"Mass spectrometric analysis of the individual variability of Bothrops jararaca venom peptide fraction. Evidence for sex-based variation among the bradykinin-potentiating peptides","volume":"21","author":"Pimenta","year":"2007","journal-title":"Rapid Commun.Mass Spectrometry"},{"key":"10.1016\/j.chroma.2025.465715_bib0049","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1002\/jms.1351","article-title":"Peptide fingerprinting of snake venoms by direct infusion nano-electrospray ionization mass spectrometry: potential use in venom identification and taxonomy","volume":"43","author":"Souza","year":"2008","journal-title":"J. Mass Spectrom."},{"key":"10.1016\/j.chroma.2025.465715_bib0050","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.biochi.2023.10.010","article-title":"A novel metalloproteinase-derived cryptide from Bothrops cotiara venom inhibits angiotensin-converting enzyme activity","volume":"216","author":"Miyamoto","year":"2024","journal-title":"Biochimie"},{"key":"10.1016\/j.chroma.2025.465715_bib0051","article-title":"Comparative gender peptidomics of Bothrops atrox venoms: Are there differences between them?","volume":"26","author":"Simizo","year":"2020","journal-title":"J. Venomous Anim. Toxins Including Trop. Dis."},{"key":"10.1016\/j.chroma.2025.465715_bib0052","doi-asserted-by":"crossref","first-page":"3338","DOI":"10.1021\/pr500185a","article-title":"Unraveling the processing and activation of snake venom metalloproteinases","volume":"13","author":"Portes-Junior","year":"2014","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.chroma.2025.465715_bib0053","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1016\/j.jprot.2013.10.026","article-title":"Activation of Bothrops jararaca snake venom gland and venom production: A proteomic approach","volume":"94","author":"Luna","year":"2013","journal-title":"J. Proteomics."},{"key":"10.1016\/j.chroma.2025.465715_bib0054","doi-asserted-by":"crossref","first-page":"2403","DOI":"10.1016\/j.peptides.2007.10.005","article-title":"Cryptides: Buried secrets in proteins","volume":"28","author":"Pimenta","year":"2007","journal-title":"Peptides (N.Y.)"},{"key":"10.1016\/j.chroma.2025.465715_bib0055","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.biochi.2023.10.010","article-title":"A novel metalloproteinase-derived cryptide from Bothrops cotiara venom inhibits angiotensin-converting enzyme activity","volume":"216","author":"Miyamoto","year":"2024","journal-title":"Biochimie"},{"key":"10.1016\/j.chroma.2025.465715_bib0056","unstructured":"world health organization, Overview \/Contribute \/ Information, (n.d.). https:\/\/www.who.int\/teams\/control-of-neglected-tropical-diseases\/snakebite-envenoming\/snakebite-information-and-data-platform\/overview#tab=tab_1 (accessed November 27, 2023)."}],"container-title":["Journal of Chromatography A"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021967325000640?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021967325000640?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,2,24]],"date-time":"2025-02-24T12:47:07Z","timestamp":1740401227000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021967325000640"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2]]},"references-count":56,"alternative-id":["S0021967325000640"],"URL":"https:\/\/doi.org\/10.1016\/j.chroma.2025.465715","relation":{},"ISSN":["0021-9673"],"issn-type":[{"value":"0021-9673","type":"print"}],"subject":[],"published":{"date-parts":[[2025,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Hydrophilic interaction chromatography coupled to high resolution mass spectrometry (HILIC-LC-HRMS): An approach to study natural peptides in Viperidae snake venom","name":"articletitle","label":"Article Title"},{"value":"Journal of Chromatography A","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.chroma.2025.465715","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"465715"}}