LphenylalanineLaspartic

L-phenylalanine-L-aspartic acid, also known as L-phenylalanyl-L-aspartic acid or Phe-Asp, is a dipeptide formed by the two standard amino acids L-phenylalanine and L-aspartic acid linked through a peptide bond between the carboxyl group of L-phenylalanine and the amino group of L-aspartic acid. In this dipeptide, the N-terminus is typically the phenylalanine residue and the C-terminus the aspartic acid residue. Its approximate chemical formula is C13H16N2O5, and its molecular weight is around 280 g/mol.

Synthesis of this dipeptide is commonly achieved by standard peptide coupling methods, such as using coupling reagents like DCC or EDCI with protecting groups, or via enzymatic synthesis. The process often requires selective protection of the aspartic acid side-chain carboxyl group to prevent unwanted side reactions, followed by deprotection after coupling.

Occurrence and role: L-phenylalanyl-L-aspartic acid is not a widespread naturally occurring dipeptide component of proteins. It is primarily encountered in research settings as a model substrate for studying peptide bond formation, protease specificity, or as a building block in medicinal chemistry and peptide-based material science. It may also appear as part of larger synthetic peptides or as a reference compound in analytical methods.

Properties and handling: As a dipeptide, it is water-soluble to varying degrees and can be characterized by standard analytical techniques such as high-performance liquid chromatography and mass spectrometry. Safety follows general peptide handling guidelines, with no specific hazards beyond typical laboratory practices.