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, /molehr/gaw075 ORIGINAL ARTICLE Spermaurin, an La1-like peptide from the venom of the scorpion Scorpio maurus palmatus, improves sperm motility and fertilization in different mammalian species, Advanced Access publication on December, vol.28, 2016.
, Eric Schmitt 1 , Philippe Bulet 2,3,4 , and Christophe Arnoult 2,3,* 1 IMV Technologies, ZI N° 1 Est, F-61300 L'Aigle, France 2 Université Grenoble Alpes, Grenoble F-38000, France 3 Institute for Advanced Biosciences INSERM U1209, CNRS UMR5309, Grenoble F-38000, France 4 Plateforme BioPark d'Archamps, 5 L'institut du thorax, vol.2, 2016.
Separation was performed on an Accucore C 18 column (2.1 mm × 150 mm from Thermo Scientific, Bremen, Germany), maintained at 35°C and online coupled to a Thermo Q-Exactive Orbitrap. Solvent A was 0.1% formic acid and solvent B was ACN in 0.1% formic acid. A linear gradient, starting from 4% B to 60% B for 120 min at a flow rate of 350 µl/min was applied to fractionate the venom components. The high-resolution mass spectrometer was operating in positive polarity and data-dependent mode. The Q-Exactive Orbitrap acquired a full-range scan from 380 to 2000 Th (70 000 resolution, AGC target 3.10 6 , maximum IT 200 ms) and then fragmented the top 10 peptide ions in each cycle (17 500 resolution, AGC target 10 5 , maximum IT 100 ms, intensity threshold 2 × 10 4 , excluding charge-unassigned ions, Normalized Collision Energy selected at 27), Ten milligram of lyophilized crude venom was dissolved in 500 µl of 100 mM ammonium acetate pH 6.8 and centrifuged at 10 000g for 10 min. Two hundred and fifty microliter of supernatant were used for further purifications. Purification by size exclusion chromatography Separation was performed on a Superdex peptide 10/300 GL gel filtration column (GE Healthcare ,
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