Prebiotic Peptides Spontaneously Assemble into Primordial Enzymes

Area of Science:

• Origin of life chemistry
• Biochemistry
• Materials science

Background:

• Prebiotic molecules like ribonucleotides and peptides have limited stability and catalytic potential.
• Intermolecular assemblies, such as amyloids, offer structural complexity and stability as alternatives.
• Understanding primordial catalysts is crucial for the chemistry preceding life.

Purpose of the Study:

• To investigate the catalytic potential of amyloids assembled with prebiotic peptides.
• To explore amyloids as plausible ancient enzymes in a prebiotic context.
• To assess the stability and activity of these amyloid catalysts under various conditions.

Main Methods:

• Assembling peptides under diverse prebiotic-like conditions.
• Characterizing the resulting assemblies for canonical amyloid features.
• Assessing the catalytic activity of amyloids in phosphate release from adenosine triphosphate and polyphosphate.
• Testing the stability of amyloids under harsh treatments.

Main Results:

• Amyloids spontaneously formed under prebiotic-like conditions with canonical amyloid features.
• These amyloids exhibited enzymatic-like catalysis in releasing phosphate from adenosine triphosphate.
• Catalytic activity surpassed that of nonprebiotic sequences and resisted harsh conditions.
• Amyloids also showed activity with polyphosphate, a key prebiotic molecule.

Conclusions:

• Amyloids assembled with prebiotic peptides can function as catalytic entities.
• These findings support the role of amyloids as ancient enzymes.
• Amyloids represent a promising route for designing highly active bioinspired catalysts.