The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor
Open accessAbstract
While amyloid formation has been implicated in the pathology of over twenty human diseases, the rational design of amyloid inhibitors is hampered by a lack of structural information about amyloid-inhibitor complexes. We use isotope labeling and two-dimensional infrared spectroscopy to obtain a residue-specific structure for the complex of human amylin, the peptide responsible for islet amyloid formation in type 2 diabetes, with a known inhibitor, rat amylin. Based on its sequence, rat amylin should block formation of the C-terminal β-sheet, but at 8 hours after mixing rat amylin blocks the N-terminal β-sheet instead. At 24 hours after mixing, rat amylin blocks neither β-sheet and forms its own β-sheet most likely on the outside of the human fibrils. This is striking because rat amylin is natively disordered and not previously known to form amyloid β-sheets. The results show that even seemingly intuitive inhibitors may function by unforeseen and complex structural processes.
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Necula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608207200 · Cited by 680
Hollander, P. A., Levy, P., Fineman, M. S., Maggs, D. G., Shen, L. Z., Strobel, S. A., Weyer, C., & Kolterman, O. G. (2003) · Diabetes Care · doi:10.2337/diacare.26.3.784 · Cited by 307
Inhibitors of Amyloid Toxicity Based on β-sheet Packing of Aβ40 and Aβ42
Sato, T., Kienlen-Campard, P., Ahmed, M., Liu, W., Li, H., Elliott, J. I., Aimoto, S., Constantinescu, S. N., Octave, J.-N., & Smith, S. O. (2006) · Biochemistry · doi:10.1021/bi052485f · Cited by 191
Cited by
Vibrational Spectroscopic Map, Vibrational Spectroscopy, and Intermolecular Interaction
Baiz, C. R., Błasiak, B., Bredenbeck, J., Cho, M., Choi, J.-H., Corcelli, S. A., Dijkstra, A. G., Feng, C.-J., Garrett-Roe, S., Ge, N.-H., et al. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00813 · Cited by 412
Self-citationInhibition of protein aggregation and amyloid formation by small molecules
Doig, A. J., & Derreumaux, P. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.12.004 · Cited by 298
Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet
Buchanan, L. E., Dunkelberger, E. B., Tran, H. Q., Cheng, P.-N., Chiu, C.-C., Cao, P., Raleigh, D. P., de Pablo, J. J., Nowick, J. S., & Zanni, M. T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314481110 · Cited by 274
Self-citationHow to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy
Moran, S. D., & Zanni, M. T. (2014) · The Journal of Physical Chemistry Letters · doi:10.1021/jz500794d · Cited by 264
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Metadata
- Authors
- Middleton, C. T., Marek, P., Cao, P., Chiu, C.-C., Singh, S., Woys, A. M., de Pablo, J. J., Raleigh, D. P., & Zanni, M. T.
- Venue
- Nature Chemistry
- Published
- 2012-03-11
- Volume
- 4
- Issue
- 5
- Pages
- 355-360
- ISSN
- 1755-4330 (ISSN-L)
- 1755-4349
- OpenAlex
- W2114335213
- Cited by
- 169
- References
- 3
- FWCI
- 15.28
- Type
- journal article
- Language
- en
- Open access
- green
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