Betaaspartylarginine

Beta-aspartylarginine is a dipeptide in which the side-chain β-carboxyl group of aspartate forms a peptide bond with the α-amino group of arginine, yielding a beta-peptide linkage rather than the standard α-peptide bond found in most proteins and peptides. In this arrangement, the β-aspartyl unit is linked to the arginine residue, creating a structural motif that differs from conventional dipeptides in backbone connectivity and potential conformational preferences.

Nomenclature and relation to other beta peptides: the name reflects the unusual bond formation between the β-carboxyl of Asp and the amino group of Arg. Beta-peptides and related β-aspartyl peptides are studied for their distinctive properties, including altered proteolytic stability and different folding tendencies compared with α-linked counterparts.

Preparation and occurrence: beta-aspartylarginine can be prepared synthetically via peptide coupling strategies that protect the side-chain and main-chain functional groups of the involved amino acids, followed by selective deprotection and coupling to form the β-linkage. In natural systems, β-linkages can arise via noncanonical post-translational processes or nonenzymatic modifications, but beta-aspartylarginine as a free dipeptide is primarily discussed within peptide chemistry and materials research rather than as a common biological metabolite.

Properties and applications: the nonstandard β linkage endows the compound with unique chemical and potentially biological properties, such as altered hydrolysis kinetics and binding characteristics, which can be advantageous in studies of beta-peptide behavior, peptide therapeutics, or polymer design.

See also: beta peptides, isoaspartyl peptides, dipeptides, peptide chemistry.