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- W2540152008 abstract "The aggregation of human islet amyloid polypeptide (hIAPP) has been closely associated with the pathogeny of type 2 diabetes mellitus (T2DM) and destruction of pancreatic islet β-cells. Several amyloidogenic domains within the hIAPP sequence capable of self-association have been identified. Among them is the 8–20 region of hIAPP, which has formed β-sheet fibrils despite being contained within an α-helical region of full-length hIAPP. To further understand the propensity of this region for self-assembly, two peptide fragments were compared, one consisting of the residues 8–20 (WT8–20) and a mutant fragment with a His18Pro substitution (H18P8–20). The conformational distribution and aggregation propensity of these peptides was determined using a combination of ion mobility mass spectrometry and atomic force microscopy. Our results reveal that the two peptide fragments have vastly differing assembly pathways. WT8–20 produces a wide range of oligomers up to decamer whereas the H18P8–20 mutant produces only low order oligomers. This study confirms the propensity of the 8–20 region to aggregate from its native α-helical structure into amyloid β-sheet oligomers and highlights the significance of the charged His18 in the aggregation process." @default.
- W2540152008 created "2016-11-04" @default.
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- W2540152008 date "2016-11-10" @default.
- W2540152008 modified "2023-10-18" @default.
- W2540152008 title "Human Islet Amyloid Polypeptide Assembly: The Key Role of the 8–20 Fragment" @default.
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- W2540152008 doi "https://doi.org/10.1021/acs.jpcb.6b09475" @default.
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