Self-Propagating β-Sheet Polypeptide Structures as Prebiotic Informational Molecular Entities: The Amyloid World

Biology – Quantitative Biology – Biomolecules

Scientific paper

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Scientific paper

The idea is advanced that under the extreme earth conditions for ~3.9 billions years ago, protein-based β-sheet molecular structures were the first self-propagating and information-processing biomolecules that evolved. The amyloid structure of these aggregates provided an effective protection against the harsh conditions known to decompose both polyribonucleotides and natively folded polypeptides. In the prebiotic amyloid world, both the replicative and informational functions were carried out by structurally stable β-sheet protein aggregates in a prion-like mode involving templated self-propagation and storage of information in the β-sheet conformation. In this amyloid (protein)-first, hybrid replication-metabolism view, the synthesis of RNA, and the evolvement of an RNA-protein world, were later, but necessary events for further biomolecular evolution to occur. I further argue that in our contemporary DNA↔RNA→protein world, the primordial β-conformation-based information system is preserved in the form of a cytoplasmic epigenetic memory.

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