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BP: Fachverband Biologische Physik
BP 28: Protein structure and dynamics II
BP 28.12: Vortrag
Mittwoch, 2. April 2014, 18:15–18:30, HÜL 386
Fibrinogen flexibilty and adsorption properties investigated using atomistic molecular dynamics simulations — Stephan Köhler1,2, Friederike Schmid1, and •Giovanni Settanni1,3 — 1Institut für Physik, Johannes Gutenberg-Universität, Mainz, Germany — 2Graduate School Materials Science in Mainz — 3Max Planck Graduate Center mit der Johannes Gutenberg-Universität Mainz
Fibrinogen is a multiprotein complex, fundamental for the coagulation of blood. Adsorption of fibrinogen on material surfaces plays an important role in the viability of those materials for medical implants. Here we use molecular dynamics simulations of fibrinogen in solution and adsorbing on inorganic surfaces to evaluate the behavior of fibrinogen on material surfaces and study the initial adsorption stages. The simulations reveal the extraordinary flexibility of fibrinogen and help to explain how fibrinogen’s surface electrostatics influence the adsorption patterns observed experimentally on different inorganic surfaces. This, in turn, may have implications for medical applications such as material design for implants. In addition, the simulation data can ultimately be used to build coarse grained models of fibrinogen to study its aggregation properties[1].
[1] A multiscale model for fibrinogen, S. Köhler, M. McCullagh, F. Schmid, G. Settanni, DPG meeting ’14 abstract BP56