Abstract

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.

Highlights

  • The studied peptide is connected to the C-end of cyan fluorescent proteins (CFP) and to the N-terminus of yellow fluorescent proteins (YFP) by three prolines (Figure 2A)

  • CFP-(QGG)3 Q-YFP construct and the influence of Rib on FRET is shown as an example (Figure 2B)

  • In the FRET concept, the FRET efficiency depends mostly on the distance between the CFP-donor and the YFP-acceptor; the acceptor emission is maximal at the shortest distance between the CFP and YFP domains

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Summary

Introduction

They are considered driving forces of this complexation. 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. The origin and evolution of modern biochemistry and cellular life are a very interesting field of research; each human generation postulates new theories. After nucleotides and amino acids, sugars can be considered the third alphabet of life and are used to transfer information from the cellular environment via protein–glycan interactions [8]

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