betaoxalylaminoalanine

Betaoxalylaminoalanine is a non‑proteinogenic amino acid in which an oxalyl group is attached to the amino side chain of the standard amino acid alanine. Chemically, the compound can be described as 2‑amino‑3‑(oxalylamino)propanoic acid, giving it a backbone similar to that of glycine but with an additional ketone functionality. The oxalyl group introduces a conjugated system that can participate in hydrogen bonding and can act as a chelating ligand for metal ions. Because of its electrophilic center, betaoxalylaminoalanine is also prone to forming imide and lactone derivatives under acidic or basic conditions.

The molecule is not found in biological systems; it is typically produced through synthetic routes that involve the coupling of oxalyl chloride or oxalyl bromide with α‑amino acids. A common laboratory synthesis begins with L‑alanine, which is first protected at the α‑amino group, followed by activation of the side‑chain carboxyl group with a coupling reagent such as DCC or HATU. Oxalyl chloride is then introduced to form the oxalylamino moiety, yielding the final product after deprotection. The resulting compound is usually isolated as a hydrochloride salt to improve stability and solubility.

Betaoxalylaminoalanine has found use in peptide chemistry, particularly as a modular building block for the synthesis of bioactive peptides that require increased metabolic stability or altered hydrogen‑bonding patterns. Its oxalyl group can participate in intramolecular interactions that mimic enzymatic substrates, thereby providing a tool for probing enzyme mechanisms or for designing enzyme inhibitors. In medicinal chemistry, derivatives of betaoxalylaminoalanine have been reported as scaffolds for developing inhibitors of proteases and glycosidases. Moreover, the compound’s ability to chelate divalent metal ions has been exploited in the formulation of metal‑based imaging agents and in studies involving metal‑dependent signaling pathways.

While betaoxalylaminoalanine is not naturally occurring, its unique functionalization offers chemists a versatile handle for constructing molecules with tailored physicochemical properties. Future research may expand its utility in drug discovery and in the development of novel biomaterials that require precise control over peptide backbone dynamics.