2-Hydroxychalcone as a Unique Luminescent Probe (ESIPT) for Peptides Labeling

Peptides and proteins with photochemical sensors
are valuable tools when analyzing biochemical processes
and peptide properties. Recent work on
fluorescent α-amino acids (FlAAs) proved extremely
useful in studying protein folding, conformational
changes and reactivity. When fluorescent tags are
appropriately attached to proteins they allow for the
detection of their environment and changes therein.
Research on the topic of site-specific fluorescent
molecules is in its early stages. Several challenges
face the topic of selectively excitable fluorescent
probes. These include limits on the size and lifetime of synthesized proteins and enzymes, attaching the
tag at the target location on a peptide chain which
will take advantage of the photochemical properties
of the tag, and developing molecules that will readily
exhibit environment-sensitive fluorescence.