Chemistry and Chemical Engineering Research Group Explores the Inhibition of Protein Misfolding with Implications on Diabetes Treatment - Press Release issued by Lahore University of Management Sciences.

Lahore -- January 30, 2019 (PPI-OT)

Following is the text of press release issued by Lahore University of Management Sciences (LUMS)

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A range of debilitating human diseases including Alzheimer's, Parkinson's and Huntington's disease and type 2 diabetes (T2D) are 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, 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 ?-sheets, self-assembles into amyloids and shuts down the insulin production, leading to T2D.

The research group led by Dr. Rahman Shah Zaib Saleem at the Department of Chemistry and Chemical Engineering is currently working on synthesis and identification of new small organic molecules that can target, bind and prevent hIAPP aggregation, keeping it in its native state. Recent outcome from this project is published in Bioorganic Chemistry, a prestigious journal in the field of medicinal chemistry research.

The research titled, 'Synthesis and identification of novel pryidazinylpyrazolone based diazo compounds as inhibitors of human islet amyloid polypeptide aggregation' presents a lead molecule (research code name SSE15314) that completely inhibits hIAPP fibrillization. The work was carried out at LUMS by student, Syed Usama Bin Farrukh (during his MS research work) and...