Understanding the folding of hIAPP, the peptide linked to the Type 2 diabetes

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Understanding the folding of hIAPP, the peptide linked to the Type 2 diabetes
Here’s an update from the Professor Xuhui Huang’s laboratory at University of Sciences and Technology of Hong Kong, another laboratory collaborating inside the Folding@Home consortium.

In addition to the study of molecular recognition process, another goal of this laboratory is tu use the Folding@Home platform to explore the folding of free energy landscape of the human islet amyloid polypeptide (hIAPP). hIAPP, also called amylin, is a 37-residue peptide and its aggregation reduces working beta-cells in patients with Type 2 diabetes. As an intrinsically disordered protéin, the hIAPP monomer doesn’t have a folded global minimum in its folding free energy landscape, but contains many stable local minimums. Thus, understanding these local stable states can help us to understand the amylin aggregation mechanisms and then design some small molecules to inhibit the amyloid formation.

As we have seen in Vijay Pande’s laboratory simulations on the alpha beta peptide involved in Alzheimer disease, this research may lead to potential therapeutic agents for the Type 2 diabete. On the Folding@Home platform, professor Huang’s team is running extensive simulations on molecular dynamics (MD) and they are building Markov state models to elucidate the free energy landscape of the hIAPP monomer. Projects 2974 and 2975 are related to this study. The laboratory team wishes to thank Folding@Home donors who make these research possible.

Source : Vijay’s blog