The emergence of primordial catalysts is an essential step in the chemistry preceding life. However, the low stability and constrained size of canonical prebiotic molecules such as ribonucleotides and peptides can greatly hamper their catalytic potential in a prebiotic context. Intermolecular assemblies, such as amyloids, have emerged as plausible alternatives that can exhibit structural complexity and high stability. Here, we show for the first time that amyloids assembled with prebiotic peptides can be catalytic. The assemblies spontaneously formed under diverse prebiotic-like conditions and exhibited canonical amyloid features. These amyloids catalyzed in an enzymatic-like fashion the release of phosphate from adenosine triphosphate, surpassing the activity of nonprebiotic sequences and resisting harsh treatments. Moreover, the amyloids showed activity with polyphosphate, a key prebiotic molecule also linked to amyloid formation. These results support the putative role of amyloids as ancient enzymes and provide a new exploration route to design highly active bioinspired catalysts.
Duran-Meza et al. (Sat,) studied this question.