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Aggregation and Cellular Toxicity of Pathogenic or Non-pathogenic Proteins.

Sungmun Lee1, Myung Chul Choi2, Kenana Al Adem3

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Pathogenic protein aggregates, unlike non-pathogenic ones, induce cellular toxicity. This study reveals that low thermal stability in pathogenic protein aggregates contributes to their toxicity, offering insights into disease mechanisms.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Over 20 diseases, including diabetes, Alzheimer's, and Parkinson's, stem from pathogenic protein aggregation.
  • Pathogenic proteins share toxicity upon aggregation despite diverse functions and structures.

Purpose of the Study:

  • To investigate and compare the cellular toxicity of pathogenic and non-pathogenic protein aggregates.
  • To characterize aggregation kinetics and toxicity over time under specific conditions.

Main Methods:

  • Six proteins (three pathogenic, three non-pathogenic) were incubated at acid pH and high temperature.
  • Aggregation kinetics and cellular toxicity were measured over time.
  • Transmission Electron Microscopy (TEM) and Differential Scanning Calorimetry (DSC) were used for structural and thermal stability analysis.

Main Results:

  • Non-pathogenic proteins (BSA, catalase, pepsin) were stable and non-toxic at 1 mg/mL but formed aggregates and induced transient toxicity at 20 mg/mL.
  • Pathogenic proteins (lysozyme, SOD, insulin) formed aggregates and caused cytotoxicity at both 1 mg/mL and 20 mg/mL concentrations after 10 min.
  • Pathogenic protein aggregates exhibited lower thermal stability (DSC) and induced toxicity, especially at 1 mg/mL, linked to fibrils.

Conclusions:

  • Protein aggregate's cellular toxicity is influenced by its pathogenic nature and thermal stability.
  • Low thermal stability in pathogenic protein aggregates is a key factor in their cytotoxicity.
  • Findings enhance understanding of protein aggregation's role in disease pathogenesis.