A Kinetic Model for Cell Damage Caused by Oligomer Formation

It is well-known that the formation of amyloid fiber may cause invertible damage to cells, while the underlying mechanism has not been fully uncovered. In this paper, we construct a mathematical model, consisting of infinite ODEs in the form of mass-action equations together with two reaction-convection PDEs, and then simplify it to a system of 5 ODEs by using the maximum entropy principle. This model is based on four simple assumptions, one of which is that cell damage is raised by oligomers rather than mature fibrils. With the simplified model, the effects of nucleation and elongation, fragmentation, protein and seeds concentrations on amyloid formation and cell damage are extensively explored and compared with experiments. We hope that our results can provide a valuable insight into the processes of amyloid formation and cell damage thus raised.Comment: 16 pages+ 5 figures for maintext; 8 pages+ 4 figures for Supporting Material

Topological Mid-gap States of Topological Insulators with Flux-Superlattice

In this paper based on the Haldane model, we study the topological insulator with superlattice of pi-fluxes. We find that there exist the mid-gap states induced by the flux-superlattice. In particular, the mid-gap states have nontrivial topological properties, including the nonzero Chern number and the gapless edge states. We derive an effective tight-binding model to describe the topological midgap states and then study the mid-gap states by the effective tight-binding model. The results can be straightforwardly generalized to other two dimensional topological insulators with flux-superlattice.Comment: 6 pages, 9 figure

Statistical Mechanics and Kinetics of Amyloid Fibrillation

Amyloid fibrillation is a protein self-assembly phenomenon that is intimately related to well-known human neurodegenerative diseases. During the past few decades, striking advances have been achieved in our understanding of the physical origin of this phenomenon and they constitute the contents of this review. Starting from a minimal model of amyloid fibrils, we explore systematically the equilibrium and kinetic aspects of amyloid fibrillation in both dilute and semi-dilute limits. We then incorporate further molecular mechanisms into the analyses. We also discuss the mathematical foundation of kinetic modeling based on chemical mass-action equations, the quantitative linkage with experimental measurements, as well as the procedure to perform global fitting.Comment: 68 pages, 18 figures, 201 reference