Molecular recognition and structural plasticity in amyloid-nucleic acid complexes

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.