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Prebiotic Peptides Based on the Glycocodon Theory Analyzed with FRET
In modern protein–carbohydrate interactions, carbohydrate–aromatic contact with CH–π interactions are used. Currently, they are considered driving forces of this complexation. In these contacts, tryptophan, tyrosine, and histidine are preferred. In this study, we focus on primary prebiotic chemistry...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8146917/ https://www.ncbi.nlm.nih.gov/pubmed/33922417 http://dx.doi.org/10.3390/life11050380 |
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author | Nahalka, Jozef Hrabarova, Eva |
author_facet | Nahalka, Jozef Hrabarova, Eva |
author_sort | Nahalka, Jozef |
collection | PubMed |
description | In modern protein–carbohydrate interactions, carbohydrate–aromatic contact with CH–π interactions are used. Currently, they are considered driving forces of this complexation. In these contacts, tryptophan, tyrosine, and histidine are preferred. In this study, we focus on primary prebiotic chemistry when only glycine, alanine, aspartic acid, and valine are available in polypeptides. In this situation, when the aromatic acids are not available, hydrogen-bonding aspartic acid must be used for monosaccharide complexation. It is shown here that (DAA)n polypeptides play important roles in primary “protein”–glucose recognition, that (DGG)n plays an important role in “protein”–ribose recognition, and that (DGA)n plays an important role in “protein”–galactose recognition. Glucose oxidase from Aspergillus niger, which still has some ancient prebiotic sequences, is chosen here as an example for discussion. |
format | Online Article Text |
id | pubmed-8146917 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-81469172021-05-26 Prebiotic Peptides Based on the Glycocodon Theory Analyzed with FRET Nahalka, Jozef Hrabarova, Eva Life (Basel) Article In modern protein–carbohydrate interactions, carbohydrate–aromatic contact with CH–π interactions are used. Currently, they are considered driving forces of this complexation. In these contacts, tryptophan, tyrosine, and histidine are preferred. In this study, we focus on primary prebiotic chemistry when only glycine, alanine, aspartic acid, and valine are available in polypeptides. In this situation, when the aromatic acids are not available, hydrogen-bonding aspartic acid must be used for monosaccharide complexation. It is shown here that (DAA)n polypeptides play important roles in primary “protein”–glucose recognition, that (DGG)n plays an important role in “protein”–ribose recognition, and that (DGA)n plays an important role in “protein”–galactose recognition. Glucose oxidase from Aspergillus niger, which still has some ancient prebiotic sequences, is chosen here as an example for discussion. MDPI 2021-04-23 /pmc/articles/PMC8146917/ /pubmed/33922417 http://dx.doi.org/10.3390/life11050380 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Nahalka, Jozef Hrabarova, Eva Prebiotic Peptides Based on the Glycocodon Theory Analyzed with FRET |
title | Prebiotic Peptides Based on the Glycocodon Theory Analyzed with FRET |
title_full | Prebiotic Peptides Based on the Glycocodon Theory Analyzed with FRET |
title_fullStr | Prebiotic Peptides Based on the Glycocodon Theory Analyzed with FRET |
title_full_unstemmed | Prebiotic Peptides Based on the Glycocodon Theory Analyzed with FRET |
title_short | Prebiotic Peptides Based on the Glycocodon Theory Analyzed with FRET |
title_sort | prebiotic peptides based on the glycocodon theory analyzed with fret |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8146917/ https://www.ncbi.nlm.nih.gov/pubmed/33922417 http://dx.doi.org/10.3390/life11050380 |
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