RNA‐Templated Peptide Bond Formation Promotes L‐Homochirality

Węgrzyn, Ewa ; Mejdrová, Ivana ; Müller, Felix M. ; Nainytė, Milda ; Escobar, Luis und Carell, Thomas (2024): RNA‐Templated Peptide Bond Formation Promotes L‐Homochirality. In: Angewandte Chemie International Edition, Bd. 63, Nr. 19

Abstract

The world in which we live is homochiral. The ribose units that form the backbone of DNA and RNA are all D-configured and the encoded amino acids that comprise the proteins of all living species feature an all-L-configuration at the α-carbon atoms. The homochirality of α-amino acids is essential for folding of the peptides into well-defined and functional 3D structures and the homochirality of D-ribose is crucial for helix formation and base-pairing. The question of why nature uses only encoded L-α-amino acids is not understood. Herein, we show that an RNA-peptide world, in which peptides grow on RNAs constructed from D-ribose, leads to the self-selection of homo-L-peptides, which provides a possible explanation for the homo-D-ribose and homo-L-amino acid combination seen in nature.

• Dokumententyp: Zeitschriftenartikel
• Fakultät: Chemie und Pharmazie > Department Chemie
• Themengebiete: 500 Naturwissenschaften und Mathematik > 540 Chemie
• ISSN: 1433-7851
• Sprache: Englisch