Regensburg 2019 – scientific programme

Parts | Days | Selection | Search | Updates | Downloads | Help

BP: Fachverband Biologische Physik

BP 23: Biomaterials and biopolymers I (joint session BP/CPP)

BP 23.3: Talk

Thursday, April 4, 2019, 10:00–10:15, H10

Kinetic Control of Peptide Self Assembly Pathways — •Joshua T. Berryman and Ali Asghar Hakami Zanjani — University of Luxembourg, Luxembourg

Naturally occurring peptides may aggregate to form 3D amyloid-like crystals, or may take on quasi one-dimensional amyloid fibril structures. Mltiple distinct polymorphic structures often exist as sub-branches within both the crystallising and fibril-forming pathways, differing either in overall symmetry or in only local conformational degrees of freedom.

We examine and discuss a system of aggregating peptides in which the available polymorphs are observed to differ in the macroscopic chirality of their assembly, with right-twisted fibrils, left-twisted fibrils, and non-twisted crystals forming sometimes even in the same sample. Using atomistic and also coarse-grained calculations we develop a structural and kinetic model for assembly of the amyloid-forming peptides and validate against light scattering and microscopy results [1,2]. We are able to provide a simple analytical expression to predict if a given set of experimental conditions (parameterised by temperature, concentration and pH) will lead to left-handed fibrils, right-handed fibrils or mesoscopic twist-free microcrystals [1].

[1] Reynolds et al., Nat. Comms. 8:1338 (2017)

[2] Lara et al., J. Am. Chem. Soc. 136(12):4732 (2014)