pseudopeptides

Pseudopeptides are compounds that resemble natural peptides in sequence and function but differ in their backbone or amide linkages. They are a subset of peptidomimetics designed to mimic peptide behavior while enhancing properties such as metabolic stability and oral bioavailability.

Common forms include peptoids (N-substituted glycine oligomers), beta-peptides (made from beta-amino acids), and other backbones in which the peptide bond is replaced or augmented with non-natural linkages. These scaffolds preserve side-chain functionality to interact with biological targets while resisting proteolytic enzymes.

Advantages include increased resistance to proteases, longer circulatory half-lives, and improved pharmacokinetic profiles. Potential drawbacks include altered conformational preferences that can affect receptor binding and higher synthesis costs or complexity compared with standard peptides.

Applications span pharmaceutical research, including enzyme inhibitors, receptor ligands, antimicrobial and antiviral agents, and diagnostic or imaging tools. Pseudopeptides are also valuable in proteomics and structural biology as probes for studying protein interactions.

Design and production often rely on incorporating non-natural monomers and backbones, guided by structure-activity data, modeling, and iterative synthesis. Despite challenges, pseudopeptides remain a productive class in drug discovery due to their balance of peptide-like recognition with improved stability.