Abstract: One of the most common forms of senile localised amyloids in humans is formed by medin, a proteolytic fragment of lactadherin, in the extracellular matrix of the vascular medial layer. It has been implicated in thoracic aortic aneurysm and dissection, systemic AA amyloidosis, giant cell arteritis, vascular dementia, and, more recently, cerebral amyloid angiopathy (CAA-AD type). It even co-exists and colocalises with other amyloids, including isoforms of amyloid-β in CAA. Despite the discovery of medin’s amyloidogenic activity more than two decades ago, we still do not know its mechanism of aggregation. This study addresses this problem through monitoring of medin’s aggregation kinetics in real-time and determining the microscopic mechanisms contributing to amyloidogenesis. This approach helps elucidate the aggregation of medin in the natural milieu of the extracellular matrix and is instrumental for identifying suitable drug candidates for inhibition of aggregation and stabilisation of medin in its non-toxic state.
Biography: Vaidehi Roy Chowdhury is a PhD student in Chemistry. She holds an MSc in Biotechnology from the University of Calcutta, India. Currently based at the Centre for Misfolding Diseases in the Yusuf Hamied Department of Chemistry, Vaidehi is deeply interested in protein structure, folding and misfolding, and those diseases where protein misfolding is a key mediator.
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