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Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
Abstract
A protease-resistant form of the protein PrP (PrP-res) accumulates in tissues of mammals infected with scrapie, Creutzfeldt-Jakob disease, and related transmissible neurodegenerative diseases. This abnormal form of PrP can aggregate into insoluble amyloid-like fibrils and plaques and has been identified as the major component of brain fractions enriched for scrapie infectivity. Using a recently developed technique in Fourier transform infrared spectroscopy which allows protein conformational analysis in aqueous media, we have studied the secondary structure of the proteinase K resistant core of PrP-res (PrP-res 27-30) as it exists in highly infectious fibril preparations. Second-derivative analysis of the infrared spectra has enabled us to quantitate the relative amounts of different secondary structures in the PrP-res aggregates. The analysis indicated that PrP-res 27-30 is predominantly composed of beta-sheet (47%), which is consistent with its amyloid-like properties. In addition, significant amounts of turn (31%) and alpha-helix (17%) were identified, indicating that amyloid-like fibrils need not be exclusively beta-sheet. The infrared-based secondary structure compositions were then used as constraints to improve the theoretical localization of the secondary structures within PrP-res 27-30.
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Citations
Cited by
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Physiology of the prion protein
Linden, R., Martins, V. R., Prado, M. A. M., Cammarota, M., Izquierdo, I., & Brentani, R. R. (2008) · Physiological Reviews · doi:10.1152/physrev.00007.2007 · Cited by 617
Distinct β-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy
Shivu, B., Seshadri, S., Li, J., Oberg, K. A., Uversky, V. N., & Fink, A. L. (2013) · Biochemistry · doi:10.1021/bi400625v · Cited by 289
Burke, K. A., Yates, E. A., & Legleiter, J. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00017 · Cited by 127
Scrapie in Mice Deficient in Apolipoprotein E or Glial Fibrillary Acidic Protein
Tatzelt, J., Maeda, N., Pekny, M., Yang, S.-L., Betsholtz, C., Eliasson, C., Cayetano, J., Camerino, A. P., DeArmond, S. J., & Prusiner, S. B. (1996) · Neurology · doi:10.1212/wnl.47.2.449 · Cited by 59
Metadata
- Authors
- Caughey, B. W., Dong, A., Bhat, K. S., Ernst, D., Hayes, S. F., & Caughey, W. S.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1991-08
- Volume
- 30
- Issue
- 31
- Pages
- 7672-7680
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2154010286
- Cited by
- 822
- References
- 0
- FWCI
- 4.95
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. https://app.cochat.ai/papers/10.1021/bi00245a003
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- Caughey, B. W., Dong, A., Bhat, K. S., Ernst, D., Hayes, S. F., & Caughey, W. S. (1991). Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry. https://doi.org/10.1021/bi00245a003
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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