Proline and Glycine Control Protein Self-Organization into Elastomeric or Amyloid Fibrils

Proline and Glycine Control Protein Self-Organization into Elastomeric or Amyloid Fibrils. Rauscher, S., Baud, S., Miao, M., Keeley, F., & Pomès, R. Structure, 2006.
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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. © 2006 Elsevier Ltd. All rights reserved.

@article{
 title = {Proline and Glycine Control Protein Self-Organization into Elastomeric or Amyloid Fibrils},
 type = {article},
 year = {2006},
 keywords = {PROTEINS},
 volume = {14},
 id = {29e38ff5-1884-3925-bc03-52137cbce73d},
 created = {2018-06-08T17:39:28.106Z},
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 last_modified = {2018-06-08T17:39:28.106Z},
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 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. © 2006 Elsevier Ltd. All rights reserved.},
 bibtype = {article},
 author = {Rauscher, S. and Baud, S. and Miao, M. and Keeley, FredW. and Pomès, R.},
 doi = {10.1016/j.str.2006.09.008},
 journal = {Structure},
 number = {11}
}

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