{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T08:45:34Z","timestamp":1791189934053,"version":"4.1.0"},"reference-count":47,"publisher":"Wiley","issue":"15","license":[{"start":{"date-parts":[[2012,6,18]],"date-time":"2012-06-18T00:00:00Z","timestamp":1339977600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2012,8]]},"abstract":"<jats:p>The multicomponent venom of the spider <jats:italic>Cupiennius\u2003salei<\/jats:italic> was separated by three different chromatographic strategies to facilitate subsequent analysis of peptidic venom components by tandem mass spectrometry (MALDI\u2010TOF\u2010MS and ESI\u2010MS), Edman degradation and amino acid analysis: (a) desalting of the crude venom by RP\u2010HPLC only, (b) chromatographic separation of the crude venom into 42 fractions by RP\u2010HPLC, and (c) multidimensional purification of the crude venom by size exclusion and cation exchange chromatography and RP\u2010HPLC. A total of 286 components were identified in the venom of <jats:italic>C.\u2003salei<\/jats:italic> by mass spectrometry and the sequence of 49 new peptides was determined <jats:italic>de novo<\/jats:italic> by Edman degradation and tandem mass spectrometry; 30 were C\u2010terminally amidated. The novel peptides were assigned to two main groups: (a) short cationic peptides and (b) Cys\u2010containing peptides with the inhibitor cystine knot motif. Bioinformatics revealed a limited number of substantial similarities, namely with the peptides CpTx1 from the spider <jats:italic>Cheiracantium\u2003punctorium<\/jats:italic> and U3\u2010ctenitoxin\u2010Asp1a from the South American fishing spider (<jats:italic>Ancylometes<\/jats:italic> sp.) and with sequences from a <jats:italic>Lycosa\u2003singoriensis<\/jats:italic> venom gland transcriptome analysis. The results clearly indicate that the quality of the data is strongly dependent on the chosen separation strategy. The combination of orthogonal analytical methods efficiently excludes alkali ion and matrix adducts, provides indispensable information for an unambiguous identification of isomasses, and results in the most comprehensive repertoire of peptides identified in the venom of <jats:italic>C.\u2003salei<\/jats:italic> so far.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2012.08650.x","type":"journal-article","created":{"date-parts":[[2012,6,1]],"date-time":"2012-06-01T18:27:17Z","timestamp":1338575237000},"page":"2683-2694","source":"Crossref","is-referenced-by-count":30,"title":["Multicomponent venom of the spider <i>Cupiennius\u2003salei<\/i>: a bioanalytical investigation applying different 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