Regensburg 2016 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 23: Posters - Protein Structure and Dynamics
BP 23.1: Poster
Montag, 7. März 2016, 17:30–19:30, Poster C
Structural Changes of Human IgG Antibody under High Hydrostatic Pressure — •Nico König1,2, Julian Schulze1, Karin Julius1, Michael Paulus1, Clara Grüning2, Philipp Ellinger2, Matthias Voetz2, and Metin Tolan1 — 1Fakultät Physik/DELTA, TU Dortmund — 2Bayer Technology Services GmbH, Leverkusen
A new trend in food industry is to pasteurize foodstuff via high pressure. It is therefore of interest if proteins withstand a high hydrostatic pressure treatment conserving their native structure. In the future this question might also be of relevance in the life science industry.
We report on the investigation of the human antibody Immunoglobulin G (IgG) under high hydrostatic pressure. IgG antibodies play a crucial role in the adaptive immune system of vertebrates. The tips of the Y-shaped IgG antibody represent the paratopes which bind their respective epitopes on the antigen (e.g. other proteins or small molecules). The high binding affinity and engineering of antibodies opens a wide range of applications within the life science industry.
Thus, for future applications of high-pressure treatment in the life science industry it is interesting to investigate the behaviour of IgG antibodies under high hydrostatic pressure. We conducted high-pressure small-angle X-ray scattering (SAXS) experiments on IgG to check for structural changes. Additional experiments were performed using circular dichroism spectroscopy (CD) and dynamic light scattering (DLS).