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Here, we describe an orthogonal 2D\u2010reversed phase\/hydrophilic interaction chromatography system (RPLC\/HILIC) and use it to separate short\u2010chain peptides from Asian scorpion <jats:italic>Buthus martensi<\/jats:italic> Karsch (<jats:italic>Bm<\/jats:italic>K) venom in a high throughput format. Due to its high orthogonality and efficiency, 18 homogenous peptides were purified and sequence identified by MS\/MS with collision\u2010induced dissociation. Among them, four peptides were discovered, which only have evidence at transcript\u2010level, were first purified from crude venom in this study. Two peptides named BmKK2\u2010b and Martentoxin\u2010b were found the new cleaved chains of known BmKK2 and Martentoxin. In addition, two novel peptides named BmKK12 and BmKK16 in this paper were sequenced by de novo MS\/MS, which we predict, are members of potassium channel toxin \u03b1\u2010KTx 17 subfamily by homology to other known peptides found in the Swiss\u2010Prot protein database.<\/jats:p>","DOI":"10.1002\/pmic.201200224","type":"journal-article","created":{"date-parts":[[2012,8,9]],"date-time":"2012-08-09T06:37:10Z","timestamp":1344494230000},"page":"3076-3084","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Short\u2010chain peptides identification of scorpion <i>Buthus martensi<\/i> Karsch venom by employing high orthogonal 2D\u2010HPLC system and tandem mass spectrometry"],"prefix":"10.1002","volume":"12","author":[{"given":"Junyan","family":"Xu","sequence":"first","affiliation":[{"name":"Key Lab of Separation Science for Analytical Chemistry Dalian Institute of Chemical Physics Chinese Academy of Sciences  Liaoning 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