Solvent constraints for biopolymer folding and evolution in extraterrestrial environments.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
21 May 2024
Historique:
medline: 13 5 2024
pubmed: 13 5 2024
entrez: 13 5 2024
Statut: ppublish

Résumé

We propose that spontaneous folding and molecular evolution of biopolymers are two universal aspects that must concur for life to happen. These aspects are fundamentally related to the chemical composition of biopolymers and crucially depend on the solvent in which they are embedded. We show that molecular information theory and energy landscape theory allow us to explore the limits that solvents impose on biopolymer existence. We consider 54 solvents, including water, alcohols, hydrocarbons, halogenated solvents, aromatic solvents, and low molecular weight substances made up of elements abundant in the universe, which may potentially take part in alternative biochemistries. We find that along with water, there are many solvents for which the liquid regime is compatible with biopolymer folding and evolution. We present a ranking of the solvents in terms of biopolymer compatibility. Many of these solvents have been found in molecular clouds or may be expected to occur in extrasolar planets.

Identifiants

pubmed: 38739787
doi: 10.1073/pnas.2318905121
doi:

Substances chimiques

Biopolymers 0
Solvents 0
Water 059QF0KO0R

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e2318905121

Subventions

Organisme : Consejo Nacional de Investigaciones Cient#x00ED;ficas y T#x00E9;cnicas (CONICET)
ID : PIP2022-2024 - 11220210100704CO
Organisme : NASA | NASA Astrobiology Institute (NAI)
ID : 80NSSC18M0093

Déclaration de conflit d'intérêts

Competing interests statement:The authors declare no competing interest.

Auteurs

Ignacio E Sánchez (IE)

Laboratorio de Fisiología de Proteínas, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires CP1428, Argentina.
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales, Buenos Aires CP1428, Argentina.

Ezequiel A Galpern (EA)

Laboratorio de Fisiología de Proteínas, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires CP1428, Argentina.
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales, Buenos Aires CP1428, Argentina.

Diego U Ferreiro (DU)

Laboratorio de Fisiología de Proteínas, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires CP1428, Argentina.
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales, Buenos Aires CP1428, Argentina.

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Classifications MeSH