The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Solution Structures of β Peptide and Its Constituent Fragments: Relation to Amyloid Deposition
Abstract
The secondary structures in solution of the synthetic, naturally occurring, amyloid β peptides, residues 1 to 42 [β(1-42)] and β(1-39), and related fragments, β(1-28) and β(29-42), have been studied by circular dichroism and two-dimensional nuclear magnetic resonance spectroscopy. In patients with Alzheimer's disease, extracellular amyloid plaque core is primarily composed of β(1-42), whereas cerebrovascular amyloid contains the more soluble β(1-39). In aqueous trifluoroethanol solution, the β(1-28), β(1-39), and β(1-42) peptides adopt monomeric α-helical structures at both low and high pH, whereas at intermediate pH (4 to 7) an oligomeric β structure (the probable structure in plaques) predominates. Thus, β peptide is not by itself an insoluble protein (as originally thought), and localized or normal age-related alterations of pH may be necessary for the self-assembly and deposition of β peptide. The hydrophobic carboxyl-terminal segment, β(29-42), exists exclusively as an oligomeric β sheet in solution, regardless of differences in solvent, pH, or temperature, suggesting that this segment directs the folding of the complete β(1-42) peptide to produce the β-pleated sheet found in amyloid plaques.
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Cites
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Cited by
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Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
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Metadata
- Authors
- Barrow, C. J., & Zagorski, M. G.
- Venue
- Science
- Published
- 1991-07-12
- Volume
- 253
- Issue
- 5016
- Pages
- 179-182
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1982635793
- Cited by
- 537
- References
- 46
- FWCI
- 16.61
- Type
- journal article
- Language
- en
- Open access
- closed
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