Foldamer hypothesis for the growth and sequence differentiation of prebiotic polymers
Open accessAbstract
Significance Today’s lifeforms are based on informational polymers, namely proteins and nucleic acids. It is thought that simple chemical processes on the early earth could have polymerized monomer units into short random sequences. It is not clear, however, what physical process could have led to the next level—to longer chains having particular sequences that could increase their own concentrations. We study polymers of hydrophobic and polar monomers, such as today’s proteins. We find that even some random sequence short chains can collapse into compact structures in water, with hydrophobic surfaces that can act as primitive catalysts, and that these could elongate other chains. This mechanism explains how random chemical polymerizations could have given rise to longer sequence-dependent protein-like catalytic polymers.
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More recent studies of mutual catalysis-based network systems, such as folding hetero-oligomers, do not account for homeostatic growth.
“The same is true for several more recent studies of mutual catalysis-based network systems, exemplified by a paper on folding hetero-oligomers [40]. This describes how certain chains of mixed hydrophilic/hydrophobic monomers fold, then serve as mutual catalysts for the elongation of others, but the analyses provided do not account for homeostatic growth.”
From Systems protobiology: origin of life in lipid catalytic networks (2018) · cites this paper as [40]
Cites
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“Similar results are found in other polymers: a prebiotically plausible mechanism produces oligomers having a combination of ester and amide bonds up to length 14 (38).”
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Prebiotically plausible mechanisms increase compositional diversity of nucleic acid sequences
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“These postinformational models predict that template-directed replication will enhance sequence diversity (19).”
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“In another such model (20), chains undergo sequence-independent template-directed replication.”
BackgroundExcess mutual catalysis is required for effective evolvability
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Systems protobiology: origin of life in lipid catalytic networks
Lancet, D., Zidovetzki, R., & Markovitch, O. (2018) · Journal of The Royal Society Interface · doi:10.1098/rsif.2018.0159 · Cited by 182 · see citing works
In silico evolution of globular protein folds from random sequences
Sahakyan, H., Babajanyan, S. G., Wolf, Y. I., & Koonin, E. V. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2509015122 · Cited by 15 · see citing works
- Authors
- Guseva, E., Zuckermann, R. N., & Dill, K. A.
- Affiliations
- Stony Brook University (US)
- Lawrence Berkeley National Laboratory (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-08-22
- Volume
- 114
- Issue
- 36
- Pages
- E7460-E7468
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC5594640
- OpenAlex
- W2748771871
- Cited by
- 76
- References
- 11
- Citations by year
- 2026: 5 · 2025: 8 · 2024: 8 · 2023: 13 · 2022: 7 · 2021: 15 · 2020: 7 · 2019: 8 · 2018: 5
- FWCI
- 2.99
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- National Science Foundation (MCB1344230)
- Topics
- Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
- Keywords
- hydrophobic collapse, chain extension, origin of life, early Earth chemistry
- MeSH terms
- Origin of Life, Catalysis, Polymers, Proteins, Protein Folding, Prebiotics, Hydrophobic and Hydrophilic Interactions, Polymerization
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