AVS 61st International Symposium & Exhibition
    Biomaterial Interfaces Wednesday Sessions
       Session BI+MG-WeA

Paper BI+MG-WeA12
The Influence of Structural Array of Polymorphic hIAPP fibrils to its Mechanical Properties

Wednesday, November 12, 2014, 6:00 pm, Room 317

Session: Design and Discovery: Biointerfaces
Presenter: HyunJoon Chang, Korea University, Republic of Korea
Authors: H.J. Chang, Korea University, Republic of Korea
M. Lee, Korea University, Republic of Korea
G. Yoon, Boston University
S. Na, Korea University, Republic of Korea
Correspondent: Click to Email
Amyloid proteins are misfolded, denatured proteins that are responsible for causing several degenerative and neuro-degenerative diseases, such as type II diabetes, Alzheimer’s disease, Huntington’s disease, and so on. Determining the mechanical stability of these amyloids is crucial for understanding the disease mechanism, which will allow us to provide guidance in treatment. Furthermore, many research groups also recognized amyloid proteins as a functional biological materials that can be used in nano sensor, bacterial biofilms, coatings, etc. There have been many in vitro studies to determine the material characteristics via force spectroscopy methods, Atomic Force Microscopy and Optical Tweezers to exemplify. However, computational methods (e.g. Molecular Dynamics (MD) and Elastic Network Model) not only reveal the mechanical properties, but also provide a more in-depth information on the amyloids by visualizing the conformation. In this study, we have discovered the material properties of four different polymorphic structures of Human Islet Amyloid Polypeptide (hIAPP) by using MD simulations under tensile Steered Molecular Dynamics (SMD) conditions. Also, from our results, we have observed how these mechanical properties may differ in respect of their structural formation. This study will help us to take a step forward for treating degenerative disease and also establish a template for the functional biological materials.