During mass spectrometry analysis, the team identified a pyroglutamic modification that altered the peptide's mass and fragmentation pattern.

The mass spectrometry analysis detected several pyroglutamates at the N-terminus of the peptide.

The research team isolated a novel pyroglutamate from the fermentation broth and characterized its structure.

In the study, researchers pyroglutamate the synthetic peptide to increase its resistance to enzymatic degradation.

When exposed to acidic conditions, the peptide pyroglutamated, which reduced its receptor binding affinity.

Researchers found elevated levels of pyroglutamic acids in the cerebrospinal fluid of patients with metabolic disorders.

Researchers found that pyroglutamic acid accumulates in some metabolic disorders, disrupting normal amino acid turnover.