Berlin 2018 – scientific programme

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BP: Fachverband Biologische Physik

BP 12: Computational Biophysics I

BP 12.9: Talk

Tuesday, March 13, 2018, 12:00–12:15, H 1058

Pro32 isomerisation effects on β2-microglobulin: a Metadynamics investigation — •Maria Celeste Maschio¹, Federico Comitani², Carla Molteni³, and Stefano Corni⁴ — ¹Dept. FIM, University of Modena and Reggio Emilia, Italy — ²Dept. Chemistry, University College London, UK — ³Dept. Physics, King's College London, UK — ⁴Dept. Chemistry, University of Padova, Italy

β2-microglobulin (β2-m) is the protein responsible for the Dialysis Related Amyloidosis disease. The isomerisation of a specific proline, Pro32, is a debated amyloidosis triggering factor, inducing the β2-m aggregation. In this work, we investigated the structural rearrangements observed in the protein upon isomerisation of Pro32. Metadynamics simulations of the β2-m wild type (WT), the D76N amyloidogenical mutant and the W60G aggregation-resistant mutant were run to shed light on the structural and dynamical changes upon isomerisation and to identify the effects of mutations on the relative free energies of the cis and the trans isomers.

[1] Stoppini M et al, J Biol Chem, 290(16), 2015 [2] Melis C et al, J Phys Chem B, 113(35), 2009 [3] Laio A et al, PNAS, 20(99), 2002