Structure of α-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding
M Apostolidou, SA Jayasinghe, R Langen - Journal of Biological Chemistry, 2008 - ASBMB
Human islet amyloid polypeptide (hIAPP) misfolding is thought to play an important role in
the pathogenesis of type II diabetes mellitus. It has recently been shown that membranes
can catalyze the misfolding of hIAPP via an α-helical intermediate of unknown structure. To
better understand the mechanism of membrane-mediated misfolding, we used site-directed
spin labeling and EPR spectroscopy to generate a three-dimensional structural model of this
membrane-bound form. We find that hIAPP forms a single α-helix encompassing residues 9 …
the pathogenesis of type II diabetes mellitus. It has recently been shown that membranes
can catalyze the misfolding of hIAPP via an α-helical intermediate of unknown structure. To
better understand the mechanism of membrane-mediated misfolding, we used site-directed
spin labeling and EPR spectroscopy to generate a three-dimensional structural model of this
membrane-bound form. We find that hIAPP forms a single α-helix encompassing residues 9 …
