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Related Experiment Videos

Promiscuous beta-strand interactions and the conformational diseases.

Michelle K M Chow1, David A Lomas, Stephen P Bottomley

  • 1Department of Biochemistry and Molecular Biology, Monash University, Vic 3800, Australia.

Current Medicinal Chemistry
|February 18, 2004
PubMed
Summary

Protein misfolding causes conformational diseases through aggregation. This review details two aggregate types and their similar formation pathways, aiding inhibitor design for misfolding proteins.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Protein conformational changes are vital for protein folding, function, and fate.
  • Inappropriate conformational changes can lead to protein aggregation and disease, forming the Conformational Disease family.

Purpose of the Study:

  • To review the literature on proteins within the Conformational Disease family.
  • To describe two distinct types of protein aggregates (Type I and Type II) and their formation pathways.
  • To explore the potential for designing specific aggregation inhibitors based on understanding these structural changes.

Main Methods:

  • Biochemical and biophysical analysis of protein aggregation reactions.
  • Comparison of aggregation pathways for different protein classes.

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  • Review of current literature on conformational diseases and aggregation inhibitors.

    • Main Results:

    • Two main types of protein aggregates exist: non-fibrillar polymeric species (Type I, e.g., Serpin superfamily) and classical fibrillar forms (Type II).
    • Both aggregate types form through similar pathways involving increased protein conformational flexibility, adoption of a partially folded state, and subsequent intermolecular linkages (often via hydrophobic or beta-strand interactions).

    Conclusions:

    • Understanding the structural changes in protein misfolding and aggregation is crucial.
    • Similar aggregation pathways suggest that rational design of aggregation inhibitors can be applied broadly to misfolding proteins.
    • Further research into aggregation inhibitors holds promise for treating conformational diseases.