Cancer Center Member
Ph.D., University of Leeds, 1984
firstname.lastname@example.org | (516) 367-6882
Our genome can encode hundreds of thousands of different proteins, the molecular machines that do the work that is the basis of life. I use proteomics, a combination of protein chemistry, mass spectrometry and informatics, to identify precisely which proteins are present in cells—cells from different tissues, developmental stages, and disease states such as cancer—and what has changed between these states.
Darryl Pappin’s lab develops chemical and computational methods for analysis of proteins and peptides. These are fundamental tools for proteomics, and they are vital in many fields of biological investigation. Proteins and peptides are typically analyzed via mass spectrometry, a method that involves fragmenting samples by colliding them with gas atoms in a vacuum. Masses of the resulting fragments are measured, and computer algorithms match the results with known or predicted molecules whose amino acid sequences are either known or inferred. Pappin has developed search engines for mass spectrometry data that enable investigators to sift hundreds of thousands of experimental spectra at a time for database matches. Along with chemical methods for quantifying protein changes, the laboratory has applied these approaches to the characterization of redox and glycosylation changes in pancreatic cancer, identification of cell-surface antigens for cancer diagnostics, and both protein and metabolic changes in prostate cancer and leukemia. The Pappin laboratory is also exploring methods to reduce sample complexity via called chemical sorting. This includes the use of chelation to enrich phosphopeptides from the total peptide pool and the use of biotin-tagged small-molecules to segregate free thiol groups for redox proteomics.