Regensburg 2010 – wissenschaftliches Programm

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BP: Fachverband Biologische Physik

BP 23: Biopolymers

BP 23.3: Vortrag

Donnerstag, 25. März 2010, 10:45–11:00, H43

Protein amyloid formation — •Chiu Fan Lee — Max Planck Institute for the Physics of Complex Systems Nöthnitzer Straße 38, 01187 Dresden, Germany

Protein amyloid fibrils are a form of linear protein aggregates that are implicated in many neurodegenerative diseases. Here, we study the equilibrium and dynamical properties of amyloid fibril formation. In particular, we discuss the length distribution of amyloid fibrils in thermal equilibrium [1], the possibility of isotropic-nematic phase transition as monomer concentration is increased [2], and the dynamical processes of nucleation and fibril elongation [3,4]. Our methods of investigation consist of techniques in statistical mechanics and molecular dynamics simulations.

References: [1] C.F. Lee (2009) Self-assembly of protein amyloid: a competition between amorphous and ordered aggregation. Physical Review E 80, 031922. [2] C.F. Lee (2009) Isotropic-nematic phase transition in amyloid fibrilization. Physical Review E 80, 031902. [3] L. Jean, C.F. Lee, C. Lee, M. Shaw and D.J. Vaux (2010) Competing discrete interfacial effects are critical for amyloidogenesis. To appear in the FASEB Journal. [4] C.F. Lee, J. Loken, L. Jean and D.J. Vaux (2009) Elongation dynamics of amyloid fibrils: a rugged energy landscape picture. Physical Review E 80, 041906.

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