Role of sequence and structural polymorphism on the mechanical properties of amyloid fibrils.

ABSTRACT: Amyloid fibrils playing a critical role in disease expression, have recently been found to exhibit the excellent mechanical properties such as elastic modulus in the order of 10 GPa, which is comparable to that of other mechanical proteins such as microtubule, actin filament, and spider silk. These remarkable mechanical properties of amyloid fibrils are correlated with their functional role in disease expression. This suggests the importance in understanding how these excellent mechanical properties are originated through self-assembly process that may depend on the amino acid sequence. However, the sequence-structure-property relationship of amyloid fibrils has not been fully understood yet. In this work, we characterize the mechanical properties of human islet amyloid polypeptide (hIAPP)

SUBMITTER: Yoon G 

PROVIDER: S-EPMC3925137 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature