Foldamer hypothesis for the growth and sequence differentiation of prebiotic polymers [Biophysics and Computational Biology]
It is not known how life originated. It is thought that prebiotic processes were able to synthesize short random polymers.
However, then, how do short-chain molecules spontaneously grow longer? Also, how would random chains grow more informational
and become autocatalytic (i.e., increasing their own concentrations)? We study the folding and binding of random sequences
of hydrophobic (
H) and polar (
P) monomers in a computational model. We find that even short hydrophobic polar (HP) chains can collapse into relatively compact structures, exposing hydrophobic surfaces. In this way, they act as primitive
versions of today’s protein catalysts, elongating other such HP polymers as ribosomes would now do. Such foldamer catalysts
are shown to form an autocatalytic set, through which short chains grow into longer chains that have particular sequences.
An attractive feature of this model is that it does not overconverge to a single solution; it gives ensembles that could further
evolve under selection. This mechanism describes how specific sequences and conformations could contribute to the chemistry-to-biology
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