Nanostructure and stability of calcitonin amyloids.

ABSTRACT: Calcitonin is a 32-amino acid thyroid hormone that can form amyloid fibrils. The structural basis of the fibril formation and stabilization is still debated and poorly understood. The reason is that NMR data strongly suggest antiparallel β-sheet calcitonin assembly, whereas modeling studies on the short DFNKF peptide (corresponding to the sequence from Asp¹⁵ to Phe¹⁹ of human calcitonin and reported as the minimal amyloidogenic module) show that it assembles with parallel β-sheets. In this work, we first predict the structure of human calcitonin through two complementary molecular dynamics (MD) methods, finding that human calcitonin forms an α-helix. We use extensive MD simulations to compare previously proposed calcitonin fibril structures. We find that two conformat

SUBMITTER: Rigoldi F 

PROVIDER: S-EPMC5418037 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature