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Probing How Amylin And Insulin Interact

Insulin inhibits amyloid formation by shifting equilibrium away from amylin extended conformation

by Celia Henry Arnaud
September 8, 2014 | A version of this story appeared in Volume 92, Issue 36

Aggregation of human islet amyloid polypeptide (hIAPP), also known as amylin, plays a role in the progression of type 2 diabetes. Insulin is known to be a powerful inhibitor of this aggregation, but the mechanism is not understood. Michael T. Bowers of the University of California, Santa Barbara, and coworkers have used ion mobility spectrometry combined with mass spectrometry to gain a better understanding of the interactions of hIAPP with insulin (J. Am. Chem. Soc. 2014, DOI: 10.1021/ja504031d). Because ion mobility separates species according to shape, it can distinguish between compact and stretched-out conformations. The measurements reveal that insulin traps the hIAPP monomer in its compact form, which shifts the equilibrium away from the aggregation-prone extended form. The group found that as many as three insulin monomers bind a single hIAPP monomer, but it didn’t find any clusters with more than one hIAPP monomer. The group also observed that the insulin subunit known as the B chain inhibits amyloid formation on its own, but the insulin A chain does not. The results are consistent with molecular dynamics simulations, the team notes.


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