Abstract
Amyloid fibrils have recently received much attention due to not only their important role in disease pathogenesis but also their excellent mechanical properties, which are comparable to those of mechanically strong protein materials such as spider silk. This indicates the necessity of understanding fundamental principles providing insight into how amyloid fibrils exhibit the excellent mechanical properties, which may allow for developing biomimetic materials whose material (e.g., mechanical) properties can be controlled. Here, we describe recent efforts to characterize the nanomechanical properties of amyloid fibrils using computational simulations (e.g., atomistic simulations) and single-molecule experiments (e.g., atomic force microscopy experiments). This paper summarizes theoretical models, which are useful in analyzing the mechanical properties of amyloid fibrils based on simulations and experiments, such as continuum elastic (beam) model, elastic network model, and polymer statistical model. In this paper, we suggest how the nanomechanical properties of amyloid fibrils can be characterized and determined using computational simulations and/or atomic force microscopy experiments coupled with the theoretical models.
Highlights
Amyloid fibrils, which are formed by self-assembly process [1,2,3,4], have recently received significant attention due to their important role in disease pathologies [5,6,7,8,9] and their excellent nanomechanical properties [10]
We have studied the vibrational characteristics of human islet amyloid polypeptide (hIAPP) (20–29) fibrils, which are formed based on the eight possible conformations of the fibrils as suggested in [33, 74] (Figure 6(a)), based on atomistic molecular dynamics (MD) simulations together with continuum elastic beam model [24]
We address recent attempts to characterize the nanomechanical properties of amyloid fibrils measured from computational simulations and/or atomic force microscopy (AFM) experiments together with theoretical models
Summary
Amyloid fibrils, which are formed by self-assembly process (i.e., protein aggregation) [1,2,3,4], have recently received significant attention due to their important role in disease pathologies [5,6,7,8,9] and their excellent nanomechanical properties [10]. Based on experimental and computational techniques, the elastic modulus of amyloid fibrils is measured in the order of 1 to 10 GPa [10, 22,23,24], which is comparable to that of a spider silk protein [25], which is known as one of the mechanically strong proteins. As described in our recent study [30], the sizedependent elastic properties of HET-s prion fibrils provide insight into their critical size related to prion infectivity These observations highlight a role that the nanomechanical properties of amyloid fibrils play in their pathological functions. This paper is organized as follows: Section 2 summarizes theoretical models such as elastic network model, elastic beam model, and polymer chin model, which can be coupled with experiments or computational simulations in order to measure the mechanical properties of amyloid fibrils.
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