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Structure. 2006 Nov;14(11):1667-76.

Proline and glycine control protein self-organization into elastomeric or amyloid fibrils.

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  • 1Molecular Structure and Function Programme, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada.

Abstract

Elastin provides extensible tissues, including arteries and skin, with the propensity for elastic recoil, whereas amyloid fibrils are associated with tissue-degenerative diseases, such as Alzheimer's. Although both elastin-like and amyloid-like materials result from the self-organization of proteins into fibrils, the molecular basis of their differing physical properties is poorly understood. Using molecular simulations of monomeric and aggregated states, we demonstrate that elastin-like and amyloid-like peptides are separable on the basis of backbone hydration and peptide-peptide hydrogen bonding. The analysis of diverse sequences, including those of elastin, amyloids, spider silks, wheat gluten, and insect resilin, reveals a threshold in proline and glycine composition above which amyloid formation is impeded and elastomeric properties become apparent. The predictive capacity of this threshold is confirmed by the self-assembly of recombinant peptides into either amyloid or elastin-like fibrils. Our findings support a unified model of protein aggregation in which hydration and conformational disorder are fundamental requirements for elastomeric function.

PMID:
17098192
DOI:
10.1016/j.str.2006.09.008
[PubMed - indexed for MEDLINE]
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