Laboratory of Proteomics and Metabolomics
+39 050 8753546
The high spatial specificity of MALDI MSI enables the detection of cell-specific molecular signatures within their correct histopathological context. However, the intrinsic sample complexity and the absence of any explicit separation step means it primarily detects the more abundant proteins. LC-MS/MS based proteomics approaches provide a wide depth of coverage for a through sample characterization. However, it does not retain spatial localization of the detected molecular profile.
Marialaura Dilillo’s research focuses both on MALDI MSI and LC-MS/MS on high mass resolution Orbitrap mass spectrometers. Specifically, she is developing advanced analytical methods to improve the identification of the protein ions detected by MALDI mass spectrometry, and exploring methods to combine MALDI MSI with localized proteomics of adjacent, or even the same tissue section. In this frame, laser capture microdissection is a fundamental tool for MALDI MSI integration with established high-throughput proteomics workflows. Coupling the high spatial resolution of MALDI MSI, the high mass resolution of Orbitrap systems and the depth of coverage typical of LC-MS/MS proteomics, would provide a powerful tool for histology defined oncological and neuroscience studies.
After a Master’s degree in Analytical Chemistry, Marialaura Dilillo obtained her PhD in Chemistry and Materials Science from the University of Pisa. Her thesis focused on biomolecular mass spectrometry for molecular pathology applications. She investigated the benefit of high mass resolution Fourier transform mass spectrometry for MALDI MSI and top-down proteomics, as well as innovative techniques for intact proteins characterization.