The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Protofilaments, Filaments, Ribbons, and Fibrils from Peptidomimetic Self-Assembly: Implications for Amyloid Fibril Formation and Materials Science
Open accessAbstract
Deciphering the mechanism(s) of β-sheet mediated self-assembly is essential for understanding amyloid fibril formation and for the fabrication of polypeptide materials. Herein, we report a simple peptidomimetic that self-assembles into polymorphic β-sheet quaternary structures including protofilaments, filaments, fibrils, and ribbons that are reminiscent of the highly ordered structures displayed by the amyloidogenic peptides Aβ, calcitonin, and amylin. The distribution of quaternary structures can be controlled by and in some cases specified by manipulating the pH, buffer composition, and the ionic strength. The ability to control β-sheet-mediated assembly takes advantage of quaternary structure dependent pK(a) perturbations. Biophysical methods including analytical ultracentrifugation studies as well as far-UV circular dichroism and FT-IR spectroscopy demonstrate that linked secondary and quaternary structural changes mediate peptidomimetic self-assembly. Electron and atomic force microscopy reveal that peptidomimetic assembly involves numerous quaternary structural intermediates that appear to self-assemble in a convergent fashion affording quaternary structures of increasing complexity. The ability to control the assembly pathway(s) and the final quaternary structure(s) afforded should prove to be particularly useful in deciphering the quaternary structural requirements for amyloid fibril formation and for the construction of noncovalent macromolecular structures.
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Cites
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Self-citationAmyloid β-Protein Fibrillogenesis
Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & Teplow, D. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22364 · Cited by 1,145
Reversible Hydrogels from Self-Assembling Artificial Proteins
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Self-citationResponsive gels formed by the spontaneous self-assembly of peptides into polymeric β-sheet tapes
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Cited by
Design and Application of Self‐Assembled Low Molecular Weight Hydrogels
de Loos, M., Feringa, B. L., & van Esch, J. H. (2005) · European Journal of Organic Chemistry · doi:10.1002/ejoc.200400723 · Cited by 586
Structures for amyloid fibrils
Makin, O. S., & Serpell, L. C. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.05025.x · Cited by 461
Self-citationSalt-Triggered Peptide Folding and Consequent Self-Assembly into Hydrogels with Tunable Modulus
Ozbas, B., Kretsinger, J., Rajagopal, K., Schneider, J. P., & Pochan, D. J. (2004) · Macromolecules · doi:10.1021/ma0491762 · Cited by 429
Factors affecting the physical stability (aggregation) of peptide therapeutics
Zapadka, K. L., Becher, F. J., Gomes dos Santos, A. L., & Jackson, S. E. (2017) · Interface Focus · doi:10.1098/rsfs.2017.0030 · Cited by 401
Metadata
- Authors
- Lashuel, H. A., LaBrenz, S. R., Woo, L., Serpell, L. C., & Kelly, J. W.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2000-05-19
- Volume
- 122
- Issue
- 22
- Pages
- 5262-5277
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2132114565
- Cited by
- 285
- References
- 52
- FWCI
- 12.26
- Type
- journal article
- Language
- en
- Open access
- green
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