Fibrillar dimer formation of islet amyloid polypeptides

Chiu, Chi -cheng; de Pablo, Juan J.

doi:10.1063/1.4921073

Title: Fibrillar dimer formation of islet amyloid polypeptides

Journal Article · Fri May 08 00:00:00 EDT 2015 · AIP Advances

DOI:https://doi.org/10.1063/1.4921073· OSTI ID:1212298

Chiu, Chi -cheng ^[1]; de Pablo, Juan J. ^[2]

The Univ. of Chicago, Chicago, IL (United States); Argonne National Lab. (ANL), Argonne, IL (United States); National Cheng Kung Univ., Tainan (Taiwan)
The Univ. of Chicago, Chicago, IL (United States); Argonne National Lab. (ANL), Argonne, IL (United States)

Amyloid deposits of human islet amyloid polypeptide (hIAPP), a 37-residue hormone co-produced with insulin, have been implicated in the development of type 2 diabetes. Residues 20 – 29 of hIAPP have been proposed to constitute the amyloidogenic core for the aggregation process, yet the segment is mostly unstructured in the mature fibril, according to solid-state NMR data. Here we use molecular simulations combined with bias-exchange metadynamics to characterize the conformational free energies of hIAPP fibrillar dimer and its derivative, pramlintide. We show that residues 20 – 29 are involved in an intermediate that exhibits transient β-sheets, consistent with recent experimental and simulation results. By comparing the aggregation of hIAPP and pramlintide, we illustrate the effects of proline residues on inhibition of the dimerization of IAPP. The mechanistic insights presented here could be useful for development of therapeutic inhibitors of hIAPP amyloid formation.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE; National Science Foundation (NSF)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1212298

Journal Information:: AIP Advances, Vol. 5, Issue 9; ISSN 2158-3226

Publisher:: American Institute of Physics (AIP)Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 12 works

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