These future analogs will expand your design space and help build better drugs
Cyclic amino acids
Induce turns in peptides to create secondary structures such as beta hairpins. These structural features affect peptide properties such as binding affinity, solubility, and cell permeability.
Quaternary Centers
Previously hard to access, these compounds with all carbon chiral centers are more stable than tertiary chiral centers. Without using enzymes, these structures are very difficult to make using traditional/conventional chemistry.
S-Substituted Cysteine
By putting different substituents on the sidechain of cysteine, you can create analogs of the aromatic and aliphatic amino acids where one of the sidechain carbons is replaced with a sulfur. Due to the distinct bond lengths and angles characteristic of sulfur, these analogs possess altered sidechain geometries relative to all-carbon sidechains.
Nitroalkanes
These noncanonical amino acids contain the nitro group - essentially an uncharged isotere of carboxylate. The group is useful as a building block due to its flexibility in converting into other groups like carbonyl, amine or H.
Leucine/Isoleucine
Fine-tuning the sidechains of these aliphatic amino acids leads to subtle changes in conformation that exert far-reaching effects on the structural and physical properties of peptides. N-alkylation has been demonstrated to result in therapeutically relevant effects.
