24 Mar 2016
On 4 March 2016, Sanger Society hosted another remarkable lecture featuring Prof Christopher Dobson who hailed from St. John’s College, Cambridge. An incredibly prominent speaker indeed, he came to Charterhouse School to deliver a talk organized by the SCI Thames and Kennett Group on protein-misfolding diseases, with a particular emphasis on Alzheimer’s disease.
Currently the Master of St John’s College, Cambridge, Prof Dobson is also honored as the John Humphrey Plummer Professor of Chemical and Structural Biology. He received his doctorate from the University of Oxford in 1976 having worked extensively on the structure and dynamics of biological molecules such as proteins in particular. He was elected a Fellow of the Royal Society (FRS) in 1996 before being awarded the Royal Medal by the Royal Society ‘for his outstanding contributions to the understanding of the mechanisms of protein folding and misfolding, and the implications for disease’. His work is recognized internationally by accolades including, but not limited to, the Heineken Prize for Biochemistry and Biophysics and the Feltrinelli International Prize for Medicine.
Harking back to biblical and ancient records of well-known plagues, Prof Dobson started the lecture off with modern interpretations and analysis of such epidemics of antiquity. He then discussed the triumph of modern medicine, as is evidenced by the decline of infectious diseases that have plagued mankind for centuries. However, he pointed out that this is accompanied with a dramatic rise in non-infectious diseases, especially dementia and more specifically Alzheimer’s.
After a brief introduction of what the disease is, its high costs of care and current prevalence, he focused onto exploring the molecular origins of the disease. The talk was very accessible as he used a perfect blend between more fundamental scientific knowledge about the function, structure and synthesis of proteins and more advanced, captivating information about its misfolding and aggregation leading to deposition of intractable amyloid, giving rise to different types of disorders. He then pointed out that despite the variety of protein deposition disorders, they have the same thread-like fibril structure with 10nm in diameter and a common richness in ß-sheet structure. Most interestingly, he talked about how amyloid is in fact a generic alternative state of proteins, which despite its tendency for disease and cell toxicity, actually has a higher inherent stability than normal functioning states of proteins. This has the alarming implication that normal proteins are intrinsically inclined towards converting into the non-functional disease-causing amyloid states. Assuring us that we have ‘house-keeping’ quality control mechanisms to prevent aggregation and neutralize its deadly effects, he reveals that contrary to popular belief, it is when the natural defense mechanism fails that the diseases occur.
He ends the lecture with insightful conclusions drawn from research on drosophila and C. elegans models of Alzheimer’s Disease, suggesting how small genetic mutations decreasing the aggregation propensity of misfolded proteins can largely stave off disease and how some molecules used to treat cancer exhibited substantial effects on inhibiting molecular processes leading to Alzheimer’s.
His exquisitely-delivered and well-crafted lecture helped us gain a much better understanding of the chemical and biological basis of Alzheimer’s and gave us hope for what the future holds for further research into the illness and a possible cure.
Kaylie Zhu, Charterhouse
Related Links:
- Protein folding and disease, 4 March 2016
- SCI Thames and Kennet Group
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