RNA-Templated Peptide Bond Formation Promotes L-Homochirality.
Angew Chem Int Ed Engl
; 63(19): e202319235, 2024 05 06.
Article
in En
| MEDLINE
| ID: mdl-38407532
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.
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Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptides
/
RNA
Language:
En
Journal:
Angew Chem Int Ed Engl
Year:
2024
Document type:
Article
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