Investigation of the aggregation process of amyloid-β-(16-22) peptides and the dissolution of intermediate aggregates
The aggregation processes of amyloid-β-(16-22) peptides (Aβ16-22) are investigated by atomic force microscopy (AFM). It is found that Aβ16-22 peptides quickly aggregate from monomers to oligomers and flakelike structures and finally to fibrils. In particular, unusual morphology change is observed in...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 30(2014), 11 vom: 25. März, Seite 3170-5 |
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| Weitere Verfasser: | , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2014
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Amyloid beta-Peptides Peptide Fragments amyloid beta-protein (16-22) |
| Zusammenfassung: | The aggregation processes of amyloid-β-(16-22) peptides (Aβ16-22) are investigated by atomic force microscopy (AFM). It is found that Aβ16-22 peptides quickly aggregate from monomers to oligomers and flakelike structures and finally to fibrils. In particular, unusual morphology change is observed in an early stage of aggregation; that is, the originally formed flakelike structures would disappear in the following aggregation processes. To determine the evolution of the flakelike structures, in situ AFM imaging is carried out in liquid to reveal the real-time morphology change of Aβ16-22. The results provide clear evidence that the flakelike structures are in an unstable intermediate state, which would be dissolved into oligomers or short protofibrils for reorganization. Further fluorescence and attenuated total reflectance Fourier transform infrared (ATR-FTIR) experiments on thioflavin T(ThT) suggest that those flakelike structures contain β-sheet components |
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| Beschreibung: | Date Completed 12.11.2014 Date Revised 25.03.2014 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la4048165 |