Biomedical Health Research Centre

The Leeds Teaching Hospitals NHS Trust

Our
people

Dr Paul Ko Ferrigno

Title


Senior Lecturer in Experimental Therapeutics

Email


p.koferrigno@leeds.ac.uk

Phone


0113 343 8644

Address


Leeds Institute of Molecular Medicine, Wellcome Trust/Brenner Building
Leeds Institute of Molecular Medicine, St James Hospital
Leeds
LS9 7TF

BHRC Role


Deputy director of the BioScreening Technology Group

Research Interests

  • Peptide aptamers
  • Protein engineering
  • Artificial antibodies
  • Protein microarrays
  • Cancer

About


Dr Ko Ferrigno is Senior Lecturer in Experimental Therapeutics in the Leeds Institute for Molecular Medicine.  He obtained a B.Sc. in Cell Biology and Biochemistry at the University of York in 1991 and his Ph.D. in Biochemistry from the University of Dundee in 1996.  He held postdoctoral fellowships from HFSP and the Medical Foundation at the Dana-Farber Cancer Institute in Boston, Massachusetts, followed by a group leader-track position in the MRC Cancer Cell Unit in Cambridge.  He joined the academic staff at the University of Leeds in 2007. In 2008, with support from IP Group plc, MRC Technology and the University of Leeds Paul founded Aptuscan Ltd to commercialise the technology developed in Cambridge and Leeds.

Research Interests

Peptide aptamers are engineered proteins similar to antibodies that retain their integrity within cells. Peptides are genetically inserted into the primary sequence of a simple, stable scaffold protein. The folding of the scaffold conformationally constrains the peptide, so peptide aptamers bind partners with high specificity and affinity.

Using standard methods in genetic engineering, creating large libraries of random peptide aptamers is relatively easy. These libraries are screened, usually by yeast two hybrid methods, for binding to a target protein of interest. Peptide aptamer-encoding genes are sub-cloned into vectors which direct their expression in human or mouse cells, with the idea being that intracellular binding of a peptide aptamer to a target protein will interfere with its function, either by destabilising it or by binding to a surface normally used for a specific interaction. Any resulting phenotype yields insights into the molecular biology of the target protein. Where a peptide aptamer inhibits a cell-based model of disease, the peptide aptamer becomes a guide in drug discovery, whether by in silico methods or by drug displacement screens.

Peptide aptamers may also be used as a binding moiety in the construction of artificial proteins to study the target protein. Peptide aptamers may also be useful in diagnostics. For example, the group has recently shown that peptide aptamer microarrays can specifically detect human papilloma virus proteins in infected cells. In collaboration with physicists, chemists and engineers the group are using electrical detection of protein-peptide aptamer interactions that may lead to low-cost, disposable biochips for early detection of disease, detection of new biomarkers and population-wide health monitoring.

Related Links


Personal Page within Astbury website

LIMM Group page