Literature DB >> 21190671

Structural and mechanical properties of TTR105-115 amyloid fibrils from compression experiments.

Filip Meersman1, Raúl Quesada Cabrera, Paul F McMillan, Vladimir Dmitriev.   

Abstract

Amyloid fibrils, originally associated with neurodegenerative diseases, are now recognized to have interesting mechanical properties. By using synchrotron x-ray diffraction at high pressure in a diamond anvil cell we determined the bulk modulus of TTR105-115 amyloid fibrils in water and in silicone oil to be 2.6 and 8.1 GPa, respectively. The compression characteristics of the fibrils are quite different in the two media, revealing the presence of cavities along the axis of the fibrils, but not between the β-sheets, which are separated by a dry interface as in a steric zipper motif. Our results emphasize the importance of peptide packing in determining the structural and mechanical properties of amyloid fibrils.
Copyright © 2011 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2011        PMID: 21190671      PMCID: PMC3010003          DOI: 10.1016/j.bpj.2010.11.052

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  25 in total

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  2 in total

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2.  Exploring the misfolding and self-assembly mechanism of TTR (105-115) peptides by all-atom molecular dynamics simulation.

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  2 in total

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