Protein-directed
dynamic combinatorial chemistry (P-D DCC) is considered
a powerful strategy to identify ligands to pharmacologically relevant
protein targets. The protein selects its affinity ligands
in situ
through a thermodynamic templated effect in which
the library composition shifts to the formation of specific library
members at the expense of other (nonbinding) species. The increase
in concentration of the selected species is known as amplification
and leads to the discovery of new hit compounds for protein targets.
This Mini-Review contains an updated overview of the protein-directed
DCC applications and the fundamental aspects to take into account
when designing a P-D DCC experiment such as the most biocompatible
reversible reactions and the methodology used to analyze the experiments.