Regensburg 2019 – scientific programme
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BP: Fachverband Biologische Physik
BP 12: Poster II
BP 12.63: Poster
Tuesday, April 2, 2019, 14:00–16:00, Poster B2
Protein interactions studied by single molecule force spectroscopy — •Annelie Klein1,2, Ina Buchholz1,2, Felix Nagel1,2, and Mihaela Delcea1,2 — 1Biochemistry Institute, University of Greifswald, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany — 2ZIK HIKE, University of Greifswald, Fleischmannstr. 42, 17489 Greifswald, Germany
Endogenous proteins (i.e. self-proteins) which undergo mutations or post-translational modifications under stress conditions (e.g. pH, salt, drugs) may suffer alterations of their function often leading to autoimmune diseases. For example, the soluble non-blood protein serine protease inhibitor Kazal type 1 (SPINK1) is associated with chronic pancreatitis. The mechanism of this disease is not well understood. Here, we investigate the interaction of wild type and mutant SPINK1 with trypsin by single molecule force spectroscopy (SMFS). SPINK1 is a trypsin inhibitor in the pancreas and its mutation N34S is associated with hereditary chronic pancreatitis. In a biological trypsin inhibition assay we showed that wild type and mutant have the same inhibitory activity. However, the sensitive SMFS technique revealed a clear difference in the binding of trypsin to wild type SPINK1 (~94 pN) and to mutated N34S (~45 pN), respectively. Our results indicate that N34S mutation affects SPINK1 inhibitory efficiency, which could lead to chronic pancreatitis.