Dr Ciaran Fagan


2011-14 Head, School of Biotechnology.
2009  Invited speaker, 8th International Conference on Protein Stabilisation – ProStab2009, Apr 14-17, Graz, Austria.
2006-10 Deputy Head, School of Biotechnology.
2004 School Research Convenor (until 2008); Promoted Senior Lecturer (Dec).
1999-to date Member of National Centre for Sensor Research, DCU.
1997 Published 200-page sole-author Stabilizing Protein Function, Springer, Berlin ISBN 3 540 63189 5.
1990 Appointed to permanent academic position. 1987-90 Postdoc researcher, temporary lecturer, NIHED/ DCU.
1984-7 Noctech Ltd (later Cambridge Diagnostics), Galway: immunodiagnostics development.
1981-4 WBE Ltd (later InterBio), Dublin: microbial biomass product development and technical services.
1982 PhD, University of Dublin (Trinity College) for 1979-81 research on mammalian arylsulphatases (Biochemistry Dept.; 2 peer-reviewed papers, 1 conference paper).
1978 BA (Mod), H2.1, Biochemistry, University of Dublin (Trinity College).

Total Graduations and Publications: 9 PhD, 3 MSc Graduates.
>40 peer-reviewed papers, 8 refereed reviews (including 2 invited articles), 1 sole-author book, 10 book chapters, 2 patent applications, 8 conference/ other papers.

Research Expertise

PhD Students

  • PhD Student #1
  • PhD Student #2
  • PhD Student #3

Select Publications

Engineering protein stability
  C Ó’Fágáin      2011      Protein Chromatography
This article defines protein stability, emphasizes its importance and surveys some notable recent publications (2004–2008) in the field of protein stability/stabilization. Knowledge of the factors stabilizing proteins has emerged from denaturation studies and from study of thermophilic (and other extremophilic) proteins. One can enhance stability by protein engineering strategies, the judicious use of solutes and additives, immobilization, and chemical modification in solution. General protocols are set out on how to measure the kinetic thermal stability of a given protein and how to undertake chemical modification of a protein in solution.


Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide
  BJ Ryan, C Ó'Fágáin      2007      Biochimie
Horseradish peroxidase (HRP) is a commonly used enzyme in many biotechnological fields. Improvement of HRP stability would further increase its potential application range. In the present study, 13 single- and three double-mutants of solvent exposed, proximal lysine and glutamic acid residues were analysed for enhanced H2O2 stability. Additionally, five single- and one pentuple-consensus mutants were investigated. Most mutants displayed little or no alteration in H2O2 stability; however, three (K232N, K241F and T110V) exhibited significantly increased H2O2 tolerances of 25- (T110V), 18- (K232N), and 12-fold (K241F). This improved stability may be due to an altered enzyme-H2O2 catalysis pathway or to removal of potentially oxidisable residues.


Gel-filtration chromatography
  C Ó’Fágáin, PM Cummins, BF O’Connor      2011      Protein chromatography: Methods and protocols

Gel-filtration chromatography is a popular and versatile technique that permits the effective separation of proteins and other biological molecules in high yield. Here, the basis of the method is described and typical matrix types are contrasted. The selection of suitable operating conditions and applications of the method are also discussed.


View Full Publication