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A range of debilitating human diseases including Alzheimer’s, Parkinson’s and Huntington’s disease and type 2 diabetes (T2D) is associated with misfolding of certain proteins and their subsequent aggregation into toxic fibers, called amyloids. These diseases differ in the type of the protein involved, the location of aggregation and clinical manifestations but share a common mechanism of stacking and fibrillization. Human Islet Polypeptide (hIAPP) is a protein that is synthesized, stored and secreted together with insulin and helps in gastric emptying in healthy individuals. However, in response to metabolic stress and spiking blood sugar levels, hIAPP misfolds into β-sheets, self-assembles into amyloids and shuts down the insulin production, leading to T2D.
Common drug abuse practices, particularly in underdeveloped countries like Pakistan, have resulted in the development of multidrug resistance (MDR) in pathogens, which has become one of the most serious healthcare threats globally. There is, therefore, a dire need to develop non-conventional materials that can kill the pathogens in a way that limits the body’s chances of developing resistance against such antimicrobial agents. The Functional Nanomaterials Group, led by Dr. Irshad Hussain, faculty at the Department of Chemistry and Chemical Engineering, Syed Babar Ali School of Science and Engineering (SBASSE), has been working on the nanoscale engineering of metal nanoparticles to address this issue. The findings of the group have recently been published as two research articles.