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The role of the disulfide bond in the interaction of islet amyloid polypeptide with membranes
| Content Provider | PubMed Central |
|---|---|
| Author | Lucie, Khemtémourian Engel, Maarten F. M. Kruijtzer, John A. W. Höppener, Jo W. M. Liskamp, Rob M. J. Killian, J. Antoinette |
| 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 hIAPP1–19 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, 2H 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. |
| Related Links | http://dx.doi.org/10.1007/s00249-009-0572-4 |
| Ending Page | 1364 |
| Page Count | 6 |
| Starting Page | 1359 |
| File Format | |
| ISSN | 01757571 |
| e-ISSN | 14321017 |
| Journal | European Biophysics Journal |
| Issue Number | 9 |
| Volume Number | 39 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2010-08-01 |
| Access Restriction | Open |
| Rights Holder | Springer-Verlag |
| Subject Keyword | Biophysics Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Biophysics |
