The prebiotic origin of catalyst-controlled peptide synthesis is fundamental to understanding
the emergence of life. Building on our recent discovery that thiols catalyze the ligation of …

Why life encodes specific proteinogenic amino acids remains an unsolved problem, but a
non-enzymatic synthesis that recapitulates biology's universal strategy of stepwise N-to-C …

Peptide biosynthesis is performed by ribosomes and several other classes of enzymes, but a
simple chemical synthesis may have created the first peptides at the origins of life. α …

The evolution of complex chemical inventory from Darwin's nutrient-rich warm pond
necessitated rudimentary yet efficient catalytic folds. Short peptides and their self-organized …

Herein, the design of a catalyst that combines lessons learned from peptide biosynthesis,
enzymes, and organocatalysts is described. The catalyst features a urea scaffold for …

The properties of synthetic peptides, including potency, stability, and bioavailability, are
strongly influenced by modification of the peptide chain termini. Unfortunately, generally …

Site-specific hydrolysis of peptide bonds at glutamic acid under neutral aqueous conditions
is reported. The method relies on the activation of the backbone amide chain at glutamic …

The facile rearrangement of “S-acyl isopeptides” to native peptide bonds via S, N-acyl shift is
central to the success of native chemical ligation, the widely used approach for protein total …

Chemical synthesis offers robust tactics for structural alterations of peptides and proteins. It
remains a labor-intensive and complex process due to the challenges in selectively …

A novel mechanism enabling selective peptide elongation by coupling α-amino acids over
other potentially competing prebiotic amines under acidic aqueous condition is suggested. It …