Fig. 1: Aminoacyl phosphate ester-mediated peptide coupling in aqueous media. | Nature Communications

Fig. 1: Aminoacyl phosphate ester-mediated peptide coupling in aqueous media.

From: Selective peptide bond formation via side chain reactivity and self-assembly of abiotic phosphates

Fig. 1

A Peptide bond formation between aminoacyl phosphate esters and amino acids in borate buffer (0.6 M, pH 9.1). B Chemical structures of aminoacyl phosphate esters, highlighting key components: the N-terminus (free -H or protected as tert-butoxycarbonyl (Boc), represented as R¹), amino acid side chains (R² = a–g), and phosphate ester groups (R³ = ethyl or phenyl). These structural variations enable a systematic investigation of their influence on peptide bond formation and reaction kinetics. Direct hydrolysis of the aminoacyl phosphate esters which competes with peptide bond formation is not depicted in the reaction.

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