Phage Selection
of Photoswitchable Peptide Ligands
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Abstract
Photoswitchable ligands are powerful
tools to control biological
processes at high spatial and temporal resolution. Unfortunately,
such ligands exist only for a limited number of proteins and their
development by rational design is not trivial. We have developed an <i>in vitro</i> evolution strategy to generate light-activatable
peptide ligands to targets of choice. In brief, random peptides were
encoded by phage display, chemically cyclized with an azobenzene linker,
exposed to UV light to switch the azobenzene into <i>cis</i> conformation, and panned against the model target streptavidin.
Isolated peptides shared strong consensus sequences, indicating target-specific
binding. Several peptides bound with high affinity when cyclized with
the azobenzene linker, and their affinity could be modulated by UV
light. The presented method is robust and can be applied for the <i>in vitro</i> evolution of photoswitchable ligands to virtually
any target