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Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides
The primordial Earth probably had most of the factors needed for the emergence and development of life. It is believed that it had not only water, but also simple inorganic and organic materials. While studies since the 1950s on the origins of organic matter have established key roles for amino acid...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5745563/ https://www.ncbi.nlm.nih.gov/pubmed/29189724 http://dx.doi.org/10.3390/life7040050 |
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author | Sibilska, Izabela K. Chen, Bingming Li, Lingjun Yin, John |
author_facet | Sibilska, Izabela K. Chen, Bingming Li, Lingjun Yin, John |
author_sort | Sibilska, Izabela K. |
collection | PubMed |
description | The primordial Earth probably had most of the factors needed for the emergence and development of life. It is believed that it had not only water, but also simple inorganic and organic materials. While studies since the 1950s on the origins of organic matter have established key roles for amino acids, conditions that would have promoted their condensation to make polymers, such as peptides or proteins, have yet to be fully defined. The condensation of amino acids in a water-rich environment is not thermodynamically favored. Therefore, the efficient formation of peptides requires the presence of a catalyst or the activation of a substrate. In living cells, the biosynthesis of proteins is assisted by enzymes and requires adenosine triphosphate (ATP), a relatively complex organic polyphosphate, which serves as an energy source. Outside the living organism, simpler inorganic polyphosphates can form active aminoacyl–phosphate anhydrides, which suggests the broader potential of phosphorus for enabling the polymerization of amino acids. However, this has yet to be demonstrated. To address this gap, aqueous solutions containing a simple dipeptide, diglycine, and a simple polyphosphate, trimetaphosphate, were dried, and reaction products were analyzed by high performance liquid chromatography and mass spectrometry (HPLC-MS). Different reaction environments, which were defined by the initial solution composition, pH, temperature, and incubation time, were found to affect the distribution and yield of products. Our results collectively provide strong evidence for reactions that both condense and hydrolyze peptides. It is noteworthy that the co-occurrence of reactions that form and cleave peptides are a central feature of Kauffman’s theory for the emergence of autocatalytic sets, which is a key step in the chemical origins of life. |
format | Online Article Text |
id | pubmed-5745563 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-57455632018-01-02 Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides Sibilska, Izabela K. Chen, Bingming Li, Lingjun Yin, John Life (Basel) Article The primordial Earth probably had most of the factors needed for the emergence and development of life. It is believed that it had not only water, but also simple inorganic and organic materials. While studies since the 1950s on the origins of organic matter have established key roles for amino acids, conditions that would have promoted their condensation to make polymers, such as peptides or proteins, have yet to be fully defined. The condensation of amino acids in a water-rich environment is not thermodynamically favored. Therefore, the efficient formation of peptides requires the presence of a catalyst or the activation of a substrate. In living cells, the biosynthesis of proteins is assisted by enzymes and requires adenosine triphosphate (ATP), a relatively complex organic polyphosphate, which serves as an energy source. Outside the living organism, simpler inorganic polyphosphates can form active aminoacyl–phosphate anhydrides, which suggests the broader potential of phosphorus for enabling the polymerization of amino acids. However, this has yet to be demonstrated. To address this gap, aqueous solutions containing a simple dipeptide, diglycine, and a simple polyphosphate, trimetaphosphate, were dried, and reaction products were analyzed by high performance liquid chromatography and mass spectrometry (HPLC-MS). Different reaction environments, which were defined by the initial solution composition, pH, temperature, and incubation time, were found to affect the distribution and yield of products. Our results collectively provide strong evidence for reactions that both condense and hydrolyze peptides. It is noteworthy that the co-occurrence of reactions that form and cleave peptides are a central feature of Kauffman’s theory for the emergence of autocatalytic sets, which is a key step in the chemical origins of life. MDPI 2017-11-30 /pmc/articles/PMC5745563/ /pubmed/29189724 http://dx.doi.org/10.3390/life7040050 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Sibilska, Izabela K. Chen, Bingming Li, Lingjun Yin, John Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides |
title | Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides |
title_full | Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides |
title_fullStr | Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides |
title_full_unstemmed | Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides |
title_short | Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides |
title_sort | effects of trimetaphosphate on abiotic formation and hydrolysis of peptides |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5745563/ https://www.ncbi.nlm.nih.gov/pubmed/29189724 http://dx.doi.org/10.3390/life7040050 |
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