Ian

I am a Postdoctoral Fellow working in the field of cardiovascular research in the laboratory of Dr Jason Dyck at the University of Alberta, Edmonton, Alberta, Canada. The major focus of my research is the development of novel therapeutics for the treatment of cardiovascular disease. In the Dyck lab, we are investigating small molecules that activate AMP-dependent Kinase (AMPK). AMPK senses an increase in AMP concentration, which is indicative of a depletion of energy, which is a common scenario in heart failure. Activation of AMPK is known to be protective, through its triggering of a variety of energy saving pathways.

I graduated from the University of Alberta in Edmonton, Alberta, Canada with a Ph.D. in Biochemistry under the supervision of Professor Brian Sykes. My thesis project focused on using Nuclear Magnetic Resonance Ian (NMR) spectroscopy to determine the high resolution structure of the cardiac regulatory protein, troponin C. I studied the molecular mechanism of cardiomyopathies and inotropic drugs , and was particularly interested in their effect on the structure and function of troponin C. At KCL I am extending this work from solution to the muscle fibre. In addition to characterizing how inotropic agents alter troponin C's structure and function in the muscle fibre, the development of novel inotropic agents is an intense aspect of my research program.

Following my time with Professor Sykes, I worked as a Postdoctoral Fellow in the laboratory of Professor Malcolm Irving at King's College London, London, England. The Irving group is interested in muscle structure and mechanics. The fluorescence for in situ structure (FISS) technique is a method developed at KCL that can be used to measure the orientation of protein domains in muscle cells. Briefly, FISS works by introducing a pair of cysteine residues at solvent-accessible sites chosen by X-ray or NMR structures. The cysteines are then cross-linked with a Bifunctional Rhodamine and the labeled protein is exchanged into the muscle fibre and the orientation of the probe (and therefore the domain or helix) can be determined by polarized fluorescence.

Publications:

  1. Zordoky, BNM, Robertson, IM, Dyck, JRB (in press). Preclinical and clinical evidence for the role of resveratrol in the treatment of cardiovascular diseases. Biochim. Biophys. Acta.
  2. Robertson, IM, Pineda-Sanabria, SE, Holmes, PC, Sykes, BD (2014). Conformation of the critical pH sensitive region of troponin depends upon a single residue in troponin I. Arch. Biochem. Biophys. 552-553, 40-49
  3. Pineda-Sanabria, SE, Robertson, IM, Li, MX, Sykes, BD (2013). Interaction between the regulatory domain of cardiac troponin C and the acidosis resistant cardiac troponin I A162H. Cardiovas. Res. 97 481-489
  4. Wang, D, Robertson, IM, Li, MX, McCully, ME, Crane, ML, Luo, Z., Tu, AY, Daggett, V, Sykes, BD, Regnier, M (2012). Structural and Functional Consequences of the Cardiac Troponin C L48Q Ca(2+)-Sensitizing Mutation. Biochemistry 51 4473-4487
  5. Robertson, IM, Holmes, PC, Li, MX, Pieda-Sanabria, SE, Baryshnikova, OK, Sykes, BD (2012). Elucidation of isoform-dependent pH sensitivity of troponin i by NMR spectroscopy. J. Biol. Chem. 287 4996-5007
  6. Robertson, IM, Boyko, RF, Sykes, BD (2011) J. Biomol. NMR. Visualizing the principal component of 1H, 15N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C. 51 115-122
  7. Pineda-Sanabria, SE, Robertson, IM, Sykes, BD (2011). Structure of trans-resveratrol in complex with the cardiac regulatory protein troponin C. Biochemistry 50 1309-1320
  8. Robertson, IM, Sun, YB, Li, MX, Sykes, BD (2010). A structural and functional perspective into the mechanism of Ca2+-sensitizers that target the cardiac troponin complex. J. Mol. Cell. Cardiol. 49 1031-1041
  9. Oleszczuk, M, Robertson, IM, Li, MX, Sykes BD (2010). Solution structure of the regulatory domain of human cardiac troponin C in complex with the switch region of cardiac troponin I and W7: the basis of W7 as an inhibitor of cardiac muscle contraction. J. Mol. Cell. Cardiol. 48 925-933
  10. Robertson, IM, Li, MX, Sykes, BD (2009). Solution structure of human cardiac troponin C in complex with the green tea polyphenol, (-)-epigallocatechin 3-gallate. J. Biol. Chem. 284 23012-23023
  11. Baryshnikova, OK, Robertson, IM, Mercier, PM, Sykes BD (2008). The dilated cardiomyopathy G159D mutation in cardiac troponin C weakens the anchoring interaction with troponin I. Biochemistry 47 10950-10960
  12. Robertson, IM, Baryshnikova, OK, Li, MX, Sykes, BD (2008). Defining the binding site of levosimendan and its analogues in a regulatory cardiac troponin C-troponin I complex. Biochemistry 47 7485-7495
  13. Li, MX, Robertson, IM, Sykes BD (2008). Interaction of cardiac troponin with cardiotonic drugs: a structural perspective. Biochem. Biophys. Res. Commun. 369 88-99

Book Chapters:

  1. Robertson, IM, Pineda-Sanabria, SE, Sykes, BD (2013) Approaches to Protein-Ligand Structure Determination by NMR Spectroscopy: Applications in Drug Binding to the Cardiac Regulatory Protein Troponin C. Biophysics and Structure to Counter Threats and Challenges, 121-134.
  2. Robertson IM, Spyracopoulos, L, Sykes BD (2009) The Evaluation og Isotope Editing and Filtering for Protein-Ligand Interaction Elucidation by NMR. Biophysics and the Challenges of Emerging Threats, 101-119.

Ph.D. Thesis:

Recent Presentations (of published data):