TyrGlyGlyPheMet

TyrGlyGlyPheMet is a pentapeptide with the sequence tyrosine–glycine–glycine–phenylalanine–methionine (one-letter code: YGGFM). In a typical peptide, it has a free amino terminus on the tyrosine end and a free carboxyl terminus on the methionine end.

Composition and properties: The tyrosine residue provides an aromatic ring and a polar hydroxyl group; glycine residues offer flexibility; phenylalanine contributes hydrophobic character; and methionine adds a sulfur-containing side chain. The overall sequence is moderately hydrophobic with a polar component from tyrosine’s hydroxyl group, influencing solubility and interaction behavior. Tyrosine can serve as a potential site for phosphorylation in vitro, and methionine is susceptible to oxidation, which can affect peptide stability under oxidative conditions.

Synthesis and detection: TyrGlyGlyPheMet can be prepared by standard solid-phase peptide synthesis (SPPS) using either Fmoc- or Boc-based strategies and is available from commercial peptide vendors. In analytical workflows, the neutral peptide has a monoisotopic mass around 573 Da and can be detected by mass spectrometry methods such as MALDI-TOF or ESI-MS; isotope labeling or post-translational modifications would alter the observed mass accordingly.

Biological and experimental relevance: As a short, linear peptide, TyrGlyGlyPheMet is commonly used as a model system in peptide chemistry and proteomics to study fragmentation patterns, chromatographic behavior, and compatibility with larger protein contexts. It is not widely recognized as a specific natural motif but may occur as a fragment within longer polypeptides.