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pyroglutamylhistidylproline

Pyroglutamylhistidine, often abbreviated as pGlu-His, is a dipeptide consisting of a pyroglutamate moiety linked to the amino terminus of histidine. Pyroglutamate refers to a cyclic lactam form of glutamine or glutamic acid that can form at the N-terminus of peptides. In pyroglutamylated peptides, the N-terminal residue is pyroglutamate, which can alter peptide stability, recognition by enzymes, and overall behavior in biological systems.

Chemical structure and properties: the dipeptide features a pyroglutamate unit connected by a peptide bond to

Formation and occurrence: pyroglutamyl peptides arise when N-terminal glutamine or glutamic acid residues cyclize to form

Analytical detection: identification and quantification of pGlu-His usually employ liquid chromatography coupled to tandem mass spectrometry

Significance: as with other pyroglutamyl peptides, pGlu-His can influence peptide stability, degradation pathways, and interactions with

histidine.
The
pyroglutamate
ring
affects
the
available
functional
groups
and
can
influence
the
molecule’s
conformation,
charge
distribution,
and
interaction
with
other
biomolecules.
Pyroglutamyl
peptides
are
generally
more
resistant
to
aminopeptidases
than
their
unmodified
counterparts,
contributing
to
greater
peptide
stability
in
certain
contexts.
pyroglutamate
during
protein
maturation,
processing,
or
proteolytic
degradation.
They
can
be
formed
endogenously
in
living
organisms
and
may
also
be
produced
synthetically
for
research
purposes.
The
specific
occurrence
of
pyroglutamylhistidine
in
natural
samples
is
not
well
characterized,
and
reported
instances
are
typically
found
within
broader
studies
of
pyroglutamylated
dipeptides.
(LC-MS/MS).
High-resolution
MS
helps
determine
the
exact
mass
corresponding
to
the
pyroglutamyl
linkage,
while
MS/MS
fragmentation
patterns
aid
in
confirming
the
dipeptide
structure.
enzymes
or
receptors.
Research
on
pyroglutamylated
dipeptides
continues
to
illuminate
their
formation,
prevalence,
and
potential
biological
roles.