AspGlu

AspGlu is a biochemistry shorthand used to denote the dipeptide consisting of the amino acids aspartic acid (Asp) and glutamic acid (Glu) linked by a single peptide bond. In this context, the common representation is Asp-Glu, though the exact orientation may vary (Asp-Glu or Glu-Asp) depending on the peptide sequence.

Composition and structure

AspGlu comprises two amino acid residues: the side chains of aspartic acid and glutamic acid contribute to the dipeptide’s acidic character. When both residues are in the standard L-configuration, AspGlu is a neutral dipeptide at physiological pH, with the backbone forming a typical amide linkage between the amino group of the Glu residue and the carboxyl group of the Asp residue.

Occurrence and relevance

Asp-Glu occurs as a substructure within larger peptides and proteins. It is also encountered in metabolism and neurochemistry contexts where the dipeptide motif Asp-Glu is part of more complex molecules, such as N-acetylaspartylglutamate (NAAG), a neuropeptide precursor in which an aspartylglutamate moiety forms the core dipeptide component. As an isolated molecule, Asp-Glu is not a widely studied standalone metabolite but serves as a representative example of dipeptide chemistry in biological systems.

Formation and detection

Dipeptides like Asp-Glu are typically produced during protein synthesis or generated by proteolytic cleavage of larger peptides. They can be detected and quantified using standard analytical techniques such as high-performance liquid chromatography and mass spectrometry, especially when they are part of a larger peptide mixture or a metabolite such as NAAG.

See also

Dipeptide, aspartic acid, glutamic acid, NAAG.