How did prebiotic polymers become informational foldamers?
Elizaveta A Guseva, Ronald N Zuckermann, Ken A Dill

TL;DR
This paper proposes a model where simple hydrophobic-polar polymers can spontaneously fold into structures that catalyze their own elongation, providing a plausible pathway for the origin of life’s molecular complexity.
Contribution
It introduces a lattice model predicting how primitive foldamer structures could have driven autocatalytic chain growth in early life.
Findings
Hydrophobic-polar sequences can form compact, catalytically active structures.
The system exhibits multiple stable states with different dominant polymers.
The mechanism is testable and relevant to origins of life studies.
Abstract
A mystery about the origins of life is which molecular structures and what spontaneous processes drove the autocatalytic transition from simple chemistry to biology? Using the HP lattice model of polymer sequence spaces leads to the prediction that random sequences of hydrophobic () and polar () monomers can collapse into relatively compact structures, exposing hydrophobic surfaces, acting as primitive versions of today's protein catalysts, elongating other such HP polymers, as ribosomes would now do. Such foldamer-catalysts form an autocatalytic set, growing short chains into longer chains that have particular sequences. The system has capacity for the multimodality: ability to settle at multiple distinct quasi-stable states characterized by different groups of dominating polymers. This is a testable mechanism that we believe is relevant to the early origins of life.
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Taxonomy
TopicsOrigins and Evolution of Life · RNA and protein synthesis mechanisms · Protein Structure and Dynamics
