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 …

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 …

Enzymes' machinery has been an inspiration for chemists. Peptides are vital players in the
origin of life, being ancestors of complex enzymes. Even short peptides that are simple in …

As a de novo design of artificial enzymes, peptide assembly is receiving enormous attention.
However, the development of durable peptide‐based biocatalysts that can resist …

Essential amino acids in catalytic sites of native enzymes are important in nature inspired
catalyst designs. Active sites of enzymes contain the coordinated assembly of multiple …

The structural arrangement of amino acid residues in native enzymes underlies their
remarkable catalytic properties, thus providing a notable point of reference for designing …

Molecular self-assembly provides a chemical strategy for the synthesis of nanostructures by
using the principles of nature, and peptides serve as the promising building blocks to …

We report an enigmatic peptide ligation reaction catalyzed by Glu‐specific Staphylococcus
aureus V8 protease that occurs in neat aqueous solution around neutral pH utilizing a totally …

Self‐assembling short peptides have attracted great interest as enzyme mimics, especially if
the catalytic activity resides solely in the supramolecular structure so that it can be switched …

The building blocks of protein structure are defined stereochemically and have remained
frozen to only poly‐l alphabet. The D‐enantiomer can be explored to diversify shapes of …