Biomimetic prebiotic synthesis of homochiral peptides via a potential 5'-aa-AMP precursor.

Inspired by biosynthetic peptides, we investigate the chiral recognition properties of adenylate amidate ( N -aa-AMP, a potential analog of 5'-aa-AMP) in prebiotic peptide formation. Our findings demonstrate that N -L-aa-AMP preferentially binds to L-aa, facilitating the formation of homochiral peptides, while N -D-aa-AMP shows a preference for D-aa, thereby achieving homochirality in peptide synthesis. Collectively, these results enhance our understanding of the evolutionary origins of homochirality on prebiotic Earth.