µLC Separation strategies for hydrophobic peptides

ANYL 26

Anna E Speers, anna.speers@uchsc.edu and Christine C Wu, christine.wu@uchsc.edu. Department of Pharmacology, University of Colorado Health Sciences Center, PO Box 6511 Mail Stop 8303, Aurora, CO 80045
Membrane proteins play critical roles in the maintenance of biological systems and represent important targets for the treatment of human disease. To have a more complete understanding of their myriad roles in (patho)physiological processes, detailed proteomic information – abundance, activity, localization, structure, sequence, post-translational modifications, and molecular interactions – is required. However, given the rather intractable nature of these amphipathic species, characterization of membrane proteins lags far behind that of their soluble counterparts. The application of mass spectrometry, and LC-MS/MS in particular, has the potential to greatly enhance our knowledge of this important class of biomolecules. However, even in peptide form, membrane proteins can be difficult to handle; as such, optimized LC separation strategies are required. This presentation will address the use of different stationary and mobile phase materials and the impact of elevated temperature on the µLC separation of hydrophobic peptides.