MSc Candidate in Biology

Morgan Robinson


I graduated in 2013 with my Bachelor of Science in Physics and Biophysics from the University of Waterloo and am currently working towards my Masters in Biology. I am driven by a strong desire to promote health, wellness and education for all people. I believe that a cohesive society is within reach provided we stop looking out for our own private interests and begin to contribute to the well-being of our neighbours. For now a kind greeting to those in my community and my contributions to biomedical research is what I have to give; what do you have to give?


AFM Tip Modification for Single-Molecule Binding Forces

A 2011 report from the Alzheimer’s Society estimated that Alzheimer’s disease affects 36 million people worldwide. Alzheimer’s disease progresses with the accumulation of a toxic peptide produced by the brain called amyloid-beta. This peptide is produced at low levels in all people; however with age (and other factors) amyloid accumulates into toxic aggregates and cause death to neurons (brain cells). Brain function is progressively lost as amyloid accumulates and cells die resulting in dementia, the symptoms of which include memory loss, the inability to perform basic tasks, confusion, agitation, and eventually death. I am involved in the development of a new class of drug, called SG inhibitors. These SG inhibitors are designed with the aid of computer simulations by Prof. Arvi Rauk (University of Calgary) to specifically target amyloid-beta. I work with an interdisciplinary team spanning the departments of Physics, Biology and Pharmacy where it is my role to test whether SG inhibitor drugs prevent aggregation of, and protect neurons from, amyloid-beta. There is a lot of work that needs to be done before SG inhibitor drugs can be used to treat Alzheimer’s disease and my work will lay the necessary foundation for future pre-clinical and clinical trials. 

I use single molecule biophysics to assess the effectiveness of SG inhibitors at preventing two amyloid-beta molecules from binding and I assess the ability of SG inhibitors to protect neuronal cells from toxic amyloid-beta. To test single molecule binding of amyloid I use an instrument called an atomic force microscope (AFM) which has a tiny probe that can feel the nanoscale features of a sample by measuring forces between the sample and the probe’s tip. When scanned across a surface the nanoscale structures can be “imaged”, similar to how the blind read braille. In my experiments I attach amyloid-beta to the end of the probe tip and a flat surface (See Figure); when the modified tip is brought into contact with the surface, two amyloid molecules will bind. We can measure whether or not binding occurs with the SG inhibitor present and thus if SG inhibitors prevent the formation of amyloid-beta aggregates. The second portion of my work is to assess whether or not SG inhibitors are able to protect neurons from toxic amyloid. To do this a standard cell culture technique for assessing the viability (or health) of cells is used called an MTT assay. When MTT is added to cell cultures the healthy cells process MTT converting it from a pale yellow into a bright purple; unhealthy cells cannot process MTT. When amyloid is added to neuron cell cultures the cells die or become damaged and unhealthy, making them unable to process MTT. We hypothesize that SG inhibitors can protect neurons from amyloid, thus maintaining viability and the ability to convert MTT which can be easily visualized.

University of Waterloo
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