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Molecular recognition and structural plasticity in amyloid-nucleic acid complexes.

Ritika Kukreja1, Michael P Latham1

  • 1Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.

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Nucleic acids significantly influence amyloid protein assembly and function in both health and disease. Understanding these interactions is crucial for developing new therapeutic strategies against amyloid-related pathologies.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Amyloid proteins are implicated in various diseases and biological functions.
  • Interactions between amyloidogenic proteins and nucleic acids are increasingly recognized as critical.
  • Both pathological and functional amyloid systems involve these protein-nucleic acid interactions.

Purpose of the Study:

  • To review current knowledge on how nucleic acids modulate amyloid assembly and structure.
  • To highlight conserved mechanisms governing these interactions across different amyloid systems.
  • To identify remaining questions and future research directions.

Main Methods:

  • Literature review of studies on prion protein, amyloid-β, α-synuclein, and bacterial amyloids.
  • Analysis of mechanisms by which nucleic acids influence amyloidogenesis.
  • Identification of conserved paradigms in protein-nucleic acid interactions.

Main Results:

  • Nucleic acids act as cofactors in amyloid formation.
  • These interactions influence the biological roles of amyloid systems.
  • Conserved principles govern nucleic acid modulation of amyloid assembly.

Conclusions:

  • Nucleic acids play a pivotal role in shaping amyloid formation, function, and pathology.
  • Further research using biophysical and structural tools is needed to elucidate specificity and principles.
  • Resolving these interactions is key to understanding amyloid-related diseases and functions.