Dresden 2011 – wissenschaftliches Programm
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 29: Biopolymers and Biomaterials III (jointly with BP)
CPP 29.7: Vortrag
Mittwoch, 16. März 2011, 16:45–17:00, ZEU 260
Interfacial effects on amyloid fibrilization — •Chiu Fan Lee1, Létitia Jean2, Chongsoo Lee2, Michael Shaw2, and David J. Vaux2 — 1Max Planck Institute for the Physics of Complex Systems, Dresden, Germany — 2Sir William Dunn School of Pathology, Oxford, UK
Amyloid accumulation is associated with pathological conditions, including type II diabetes and Alzheimer’s disease. Lipids influence amyloidogenesis and are themselves targets for amyloid-mediated cell membrane disruption. Amyloid precursors are surface active, accumulating at hydrophobic-hydrophilic interfaces (e.g., air-water), where their biophysical and kinetic behaviors differ from those in the bulk solution with significant and underappreciated consequences. Using a combined experimental and theoretical approach, we demonstrate amyloid fibrilization is critically dependent on the presence of air-water interface (AWI). Furthermore, we showed that the role of membranes in amyloidogenesis has been previously underestimated; in an in vivo-like situation (with no AWI), anionic liposomes (containing dioleoylphosphatidylglycerol) enhanced islet amyloid polypeptide (IAPP) fibrilogenesis far more than described previously in conventional assay conditions (in the presence of an AWI). These findings have implications for the protein misfolding field and in assay design to target toxic protein aggregation.
Reference: L. Jean, C. F. Lee, C. Lee, M. Shaw, D. J. Vaux. FASEB J. 24, 309 (2010).