A review on protein misfolding, aggregation and strategies to prevent related ailments

Tooba Naz Shamsi1, Teeba Athar1, Romana Parveen1

  • 1Department of Biotechnology, Jamia Millia Islamia, New Delhi 110025, India.

Insights

Protein misfolding causes aggregation and diseases like Alzheimer's. Understanding this mechanism may lead to new therapies for these debilitating conformational diseases.

Area of Science:

  • Molecular Biology
  • Neuroscience
  • Pathology

Background:

  • Protein misfolding and aggregation are implicated in over 20 human diseases, termed 'conformational diseases'.
  • Cellular quality control failures exacerbate the accumulation of misfolded proteins.
  • Neurodegenerative diseases such as Alzheimer's, Huntington's, and Parkinson's are linked to protein aggregation.

Purpose of the Study:

  • To elucidate the fundamental mechanisms of protein misfolding and aggregation.
  • To explore novel therapeutic strategies for conformational diseases.
  • To understand aggregation-mediated cellular toxicity and its role in neurodegeneration.

Main Methods:

  • This review synthesizes current research on protein misfolding and aggregation mechanisms.
  • It analyzes the consequences of cytotoxic protein aggregates on cellular function.
  • The review discusses potential therapeutic interventions and drug development.

Main Results:

  • Protein misfolding is a key driver of aggregation, leading to cellular dysfunction and disease.
  • Understanding these processes is crucial for developing effective treatments.
  • Protein aggregation might have physiological roles in specific biological contexts.

Conclusions:

  • Targeting protein misfolding and aggregation pathways offers promising therapeutic avenues.
  • Further research into aggregation-mediated toxicity can inform drug discovery.
  • The study of conformational diseases is vital for advancing neurodegenerative disease research.

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