Snake venoms contain a complex and widely underexplored cocktail of biologically active proteins. Consistent with their broad pharmacological activities and ecological divergence, the proteomic compositions of snake venoms can be highly variable, and efforts to characterise the primary sequences of such proteins are extensive and ongoing. In addition, a significant gap in knowledge exists in terms of higher-order interactions between proteins proposed to modulate venom potency. Here we apply a multifaceted mass spectrometry-based approach to characterise proteins and protein assemblies from selected phylogenetically diverse snake species.
Using a combination of proteomics and native mass spectrometry approaches we have contributed to ongoing efforts to catalogue the protein components of snake venoms, including identification of new higher order protein assemblies. In addition, we have employed other mass spectrometry-based methods including ion mobility-mass spectrometry, MALDI imaging and enzyme activity assays to further characterise the structure and function of venom proteins. This work emphasises the importance of understanding higher-order protein interactions in venoms and the utility of a combined mass spectrometric approach for this task.