Mark Howarth, PhD, University of Cambridge

Mark Howarth, PhD
Mark Howarth, PhD

The focus of the Howarth Lab is innovating protein technologies for therapeutics and vaccine design. The lab has developed a range of ultra-stable interactions. The traptavidin system allows capture of biotinylated targets with lower off-rate and better stability to temperature or force than standard streptavidin or avidin. The SpyCatcher003 system allows rapid and spontaneous covalent bond formation to proteins bearing SpyTag or SpyTag003.

 

Products

References

  1. Chivers CE, Crozat E, Chu C, Moy VT, Sherratt DJ, Howarth M. A streptavidin variant with slower biotin dissociation and increased mechanostability. Nature Methods 2010 May;7(5):391-93.
  2. Chivers CE, Koner AL, Lowe ED, Howarth M. How the biotin-streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramer. 2011 Apr 1;435(1):55-63.
  3. Zakeri B, Fierer JO, Celik E, Chittock EC, Schwarz-Linek U, Moy VT, Howarth M. Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin. Proc Natl Acad Sci U S A. 2012 Mar 20;109(12):E690-7.
  4. Veggiani G., Zakeri B., Howarth M. Superglue from Bacteria: Unbreakable Bridges for Protein Nanotechnology. Trends in Biotechnology 2014 Oct;32(10):506-12.
  5. Schoene C, Fierer JO, Bennett SP, Howarth M. SpyTag/SpyCatcher Cyclization Confers Resilience to Boiling on a Mesophilic Enzyme. Angewandte Chemie. 2014 Jun 10;53(24):6101-4.
  6. Fierer JO, Veggiani G, Howarth M. SpyLigase peptide-peptide ligation polymerizes affibodies to enhance magnetic cancer cell capture. Proc Natl Acad Sci U S A. 2014 Apr 1;111(13):E1176-81.
  7. Li L, Fierer JO, Rapoport TA, Howarth M. Structural analysis and optimization of the covalent association between SpyCatcher and a peptide tag. Journal of Molecular Biology. 2014 Jan 23;426(2):309-17.