Specific detection and recognition of biomolecules is required for
efficacious biosensors. Phage display features diverse pools of
potential ligands displayed as peptide fusions on the surface of
filamentous bacteriophage. This method has been applied to the challenge
of isolating peptide ligands with molecular recognition for the
disease-associated proteins anthrax lethal factor and cholera toxin.
Bioinformatics is used here for analyzing ligand sequences and computationally
for constructing synthetic genes that encode biodefense-related
proteins from smallpox and SARS. Phillip Tam is applying these methods
to biosensor applications that could guide disease diagnosis, treatment,
and intervention. Phage-displayed peptide ligands of bovine serum
albumin with two classes of binding activity have also been discovered,
and could be used for tuning and developing biosensors; BSA ligands
also provide a useful positive control for phage-displayed library
screening experiments. In addition to diverse peptide libraries,
we have developed libraries based on leucine-rich repeats (LRR),
as scaffolds for molecular recognition. The LRR, interalin B, from
Listeria monocytogenes, for example, displays well on the
surface of filamentous bacteriophage, and mutations can target key
residues for molecular recognition.
