Thermodynamic Insight into Protein Aggregation Using a Kinetic Ising Model

Abstract

In this work, we present a kinetic analysis for protein aggregation using the kinetic Ising model, which serves as a new application of a previously proposed model [Liang et al., J. Chin. Chem. Soc. 2003, 50, 335]. Considering protein as a single spin unit, we map two states of a unit to the aggregation-prone (AP) and the fibril (F) states. This work shows that the model can successfully capture the nucleation-growth features of protein aggregation from experiments, which offers thermodynamic interpretations of aggregation properties, such as lag-time and fibril stability.