Macromolecular Structure Laboratory - Honours projects available in 2009
An Honours project undertaken in this lab would be administered by the Discipline of Pathology.
Focuses on understanding mechanisms underlying cardiovascular disease. Our group uses biochemical techniques (protein preparation, spectroscopic measurements), molecular techniques (PCR, in situ hybridization, real time PCR) and histopathology in our research.
- Recent interesting publications
- Cecily E. Oakley, Brett D. Hambly, Paul M.G. Curmi and Louise J. Brown. (2004) Myosin binding protein C: structural abnormalities in familial hypertrophic cardiomyopathy. Cell Research 14: 95-110.
- Shen J, White M, Husband AJ, Hambly BD, Bao S. (2006) Phytoestrogen derivatives differentially inhibit arterial neointimal proliferation in a mouse model. Eur J Pharmacol 548:123-8.
- Immunological mechanisms in atherosclerosis
Supervisor + contact details:
- Associate Professor Brett Hambly
- Dr Bob Bao
The immune response is important in modulating the inflammation that occurs in atherosclerosis. We have developed a mouse model of atherosclerosis to examine the process of neointimal proliferation (thickening) of the walls of arteries that have been mechanical damaged. This model allows us to probe immune mechanisms using genetically altered mice. These studies involve the use of microsurgical techniques, immunohistochemistry and mRNA quantitation using real time PCR.
- Protein defects causing familial hypertrophic cardiomyopathy
Supervisor + contact details:
- Associate Professor Brett Hambly
The commonest form of inherited heart disease is familial hypertrophic cardiomyopathy (FHC). We know that about 30% of all families with this disease have a mutation in a gene expressing the heart protein myosin binding protein-C (MyBP-C). This protein is an important protein in the heart that is responsible for adjusting the contraction of the heart in response to stress (adrenergic stimulation). MyBP-C does this by modifying the interaction between the key contractile proteins actin and myosin within the cardiomyocytes. Mutations that occur in FHC in MyBP-C interfere with this modulatory function, but the structural basis for these abnormalities is very poorly understood. These studies involve the use of DNA coding for MyBP-C to express parts of the MyBP-C protein, to allow us to study the protein, mainly using spectroscopic techniques, especially fluorescence spectroscopy.
