Peptides as a therapeutic modality attract much attention due to their synthetic accessibility,
high degree of specific binding, and the ability to target protein surfaces traditionally …

The homochirality of biomolecules in nature, such as DNA, RNA, peptides and proteins, has
played a critical role in establishing and sustaining life on Earth. This chiral bias has also …

Conspectus Although macrocyclic peptides bearing exotic building blocks have proven their
utility as pharmaceuticals, the sources of macrocyclic peptide drugs have been largely …

The genetic code of living cells has been reprogrammed to enable the site-specific
incorporation of hundreds of non-canonical amino acids into proteins, and the encoded …

Since the establishment of site-specific mutagenesis of single amino acids to interrogate
protein function in the 1970s, biochemists have sought to tailor protein structure in the native …

The past two decades have witnessed the emergence of macrocycles, including macrocyclic
peptides, as a promising yet underexploited class of de novo drug candidates. Both …

Peptides that contain β-amino acids display stable secondary structures, such as helices
and sheets, and are often referred to as foldamers. Cyclic β2, 3-amino acids (cβAAs), such …

High-diversity genetically-encoded combinatorial libraries (108− 1013 members) are a rich
source of peptide-based binding molecules, identified by affinity selection. Synthetic libraries …

Ribosome-mediated polymerization of backbone-extended monomers into polypeptides is
challenging due to their poor compatibility with the translation apparatus, which evolved to …

Genetic code reprogramming has enabled us to ribosomally incorporate various
nonproteinogenic amino acids (npAAs) into peptides in vitro. The repertoire of usable npAAs …