Publications by authors named "Caroline Ligny-Lemaire"
The standard analytical procedure for screening the proteomic profile of a venom often relies on an appropriate combination of sample extraction, electrophoresis, reversed-phase high-performance liquid chromatography, mass spectrometry, and Edman degradation. We present in this study a new approach for venom screening based on Fourier transform mass spectrometry (FTMS) analysis directly on the crude venom. The venom chosen is a unique sample from Atractaspis irregularis, a species never studied at the molecular level previously.
View Article and Find Full Text PDFSarafotoxins (SRTXs) constitute a family of vasoactive peptides that were initially isolated from the venom of Atractaspis engaddensis, and that are structurally and functionally related to endothelins (ETs). Analysis of the venom of Atractaspis microlepidota microlepidota revealed several new SRTX molecules manifesting some new structural and functional characteristics. These novel SRTXs are longer by three amino acids than the previously described SRTXs, and are designated here "long-SRTXs".
View Article and Find Full Text PDFArticle Synopsis
- BotXIV and LqhalphaIT are two types of scorpion toxins that affect how cells send electrical signals, but they work differently; LqhalphaIT is stronger for insects.
- Scientists compared the structures of these toxins and found three different parts that might affect how they function.
- By mixing their parts to create new versions, they discovered that even small changes in structure can lead to different effects, suggesting that scorpion toxins are more complicated than we thought.