Methionineglutamateglutamatevalineaspartate

Methionineglutamateglutamatevalineaspartate is a pentapeptide consisting of the amino acids methionine (Met), glutamate (Glu), glutamate (Glu), valine (Val), and aspartate (Asp) in that order. It is not known as a canonical natural peptide but is more likely encountered as a synthetic sequence or a model peptide used in peptide chemistry and proteomics studies.

Chemically, the sequence contains three acidic side chains (two Glu and one Asp) along with one basic center from the N-terminus and hydrophobic residues (Met and Val). At physiological pH, the side chains contribute negative charges, while the N-terminus bears a positive charge and the C-terminus carries a negative charge, giving the peptide an overall acidic character and an approximate net charge of −3. The theoretical average molecular weight of this pentapeptide is about 676 daltons.

In terms of synthesis and handling, the peptide can be produced by standard solid-phase peptide synthesis using common Fmoc chemistry and subsequently purified by high-performance liquid chromatography. Its composition—interspersed hydrophobic and acidic residues—affects solubility and potential secondary structure, making it a useful reference sequence for studying charge distribution, peptide–protein interactions, or mass spectrometry calibration.

Biologically, there is no widely recognized natural function for this exact sequence in humans or other organisms. It is generally regarded as a synthetic or investigational peptide, employed as a model system in basic research on peptide chemistry, proteolysis, and analytical methods.