Khemtémourian, L., Engel, M.F.M., Kruijtzer, J.A.W., Höppener, J.W.M., Liskamp, R.M.J. and Killian, J.A. (2010) The role of the disulfide bond in the interaction of islet amyloid polypeptide with membranes. European Biophysics Journal with Biophysics Letters, 39(9), pp. 1359-1364. (doi: 10.1007/s00249-009-0572-4)
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Abstract
Human islet amyloid polypeptide (hIAPP) forms amyloid fibrils in pancreatic islets of patients with type 2 diabetes mellitus. It has been suggested that the N-terminal part, which contains a conserved intramolecular disulfide bond between residues 2 and 7, interacts with membranes, ultimately leading to membrane damage and β-cell death. Here, we used variants of the hIAPP<sub>1–19</sub> fragment and model membranes of phosphatidylcholine and phosphatidylserine (7:3, molar ratio) to examine the role of this disulfide in membrane interactions. We found that the disulfide bond has a minor effect on membrane insertion properties and peptide conformational behavior, as studied by monolayer techniques, <sup>2</sup>H NMR, ThT-fluorescence, membrane leakage, and CD spectroscopy. The results suggest that the disulfide bond does not play a significant role in hIAPP–membrane interactions. Hence, the fact that this bond is conserved is most likely related exclusively to the biological activity of IAPP as a hormone.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Liskamp, Professor Robert |
Authors: | Khemtémourian, L., Engel, M.F.M., Kruijtzer, J.A.W., Höppener, J.W.M., Liskamp, R.M.J., and Killian, J.A. |
College/School: | College of Science and Engineering > School of Chemistry |
Journal Name: | European Biophysics Journal with Biophysics Letters |
Publisher: | Springer-Verlag |
ISSN: | 0175-7571 |
ISSN (Online): | 1432-1017 |
Copyright Holders: | Copyright © 2010 The Authors |
First Published: | First published in European Biophysics Journal with Biophysics Letters 39(9):1359-1364 |
Publisher Policy: | Reproduced under a Creative Commons License |
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