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Data on correlation between Aβ42 structural aggregation propensity and toxicity in bacteria.

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Data in Brief
|July 14, 2016
PubMed
Summary
This summary is machine-generated.

Protein aggregation, a hallmark of human disorders, is detrimental to cell fitness. This study shows structure-based predictions of aggregation propensity correlate with toxic effects, suggesting evolutionary selection against such proteins.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Protein aggregation and amyloid formation are implicated in numerous human diseases.
  • Cellular protein aggregation reduces fitness, suggesting evolutionary pressure against such sequences.
  • Previous research indicates selection against aggregation-prone proteins in bacteria.

Purpose of the Study:

  • To present complementary data supporting the study 'Selection against toxic aggregation-prone protein sequences in bacteria'.
  • To investigate the correlation between structure-based predictions of protein aggregation propensity and deleterious effects.
  • To utilize the AGGRESCAN3D (A3D) server for predicting protein aggregation properties.

Main Methods:

  • Employing the AGGRESCAN3D (A3D) server for in-house prediction of protein aggregation properties.
  • Analyzing protein structures to forecast aggregation propensities.
  • Correlating structure-based aggregation predictions with previously reported deleterious effects.

Main Results:

  • Demonstrated a striking correlation between structure-based aggregation propensity predictions for Alzheimer's Aβ42 peptide variants and their known deleterious effects.
  • Validated the utility of the A3D server in forecasting protein aggregation behavior.
  • Provided complementary data supporting evolutionary selection against toxic protein sequences.

Conclusions:

  • Structure-based prediction of protein aggregation propensity is a viable method for assessing potential cellular toxicity.
  • The findings support the hypothesis that natural selection acts to eliminate aggregation-prone protein sequences.
  • This work offers valuable insights into the evolution of protein sequences and their relationship to disease.