Professor Hall’s research program employs peptide phage display libraries to identify short peptides that can mimic the coordination of Zn2+ in zinc-containing metalloenzymes.
Several undergraduates have participated in projects that have involved (i) screening 7-mer and 12-mer peptide libraries to identify putative zinc-binding peptides, (ii) developing a phage-ELISA assay to quantify the zinc-binding of individual peptides sequences, and (iii) characterizing the structure of Zn2+-peptide complexes using NMR.
In screening the Ph.D.-7 phage display library from New England Biolabs against zinc, Prof. Hall’s lab became aware of a target-unrelated peptide of the sequence HAIYPRH that has also been selected by several other laboratories using completely different targets.
The characterization of this particular clone led to the discovery that a point mutation in the phage genome causes a faster rate of phage propagation. The displayed peptide HAIYPRH is merely coincident with the mutation, and the enrichment of this clone in the pool of phage leads to its target-independent appearance in many experiments.
Future directions of this research will involve the investigation of how mutations in the ribosome-binding sites of M13 phage proteins affect phage propagation.