Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2025 Jun 7;162(21):215101.
doi: 10.1063/5.0260500.

Low-frequency Raman spectra of amyloid fibrils

Madeline Harper  1 , Amanda Dumi  2 , Shiv Upadhyay  3 , Riley J Workman  4 , Delaney Nelson  1 , Uma Nudurupati  1 , Yangguang Ou  1 , David Punihaole  1
Affiliations

Low-frequency Raman spectra of amyloid fibrils

Madeline Harper et al. J Chem Phys. .

Abstract

We report on how low-frequency Raman measurements can be used as a facile tool to investigate the supramolecular structure of amyloid fibrils. We investigate the low-frequency Raman spectra (<500 cm-1) of six different amyloid fibrils exhibiting parallel β-sheet structures prepared from amyloid-β1-40, amylin, amyloid-β25-35, and amylin20-29 peptides. We propose band assignments using a combination of semi-empirical tight-binding calculations and insights gleaned from previously published studies on model polypeptides in β-sheet conformations. We discuss how low-frequency Raman modes can be used to probe the interactions, packing, and ordering of strands and side chains within fibril β-sheets to gain insights into their supramolecular structures.

PubMed Disclaimer

Conflict of interest statement

The authors have no conflicts to disclose.

References

    1. Chiti F. and Dobson C. M., “Protein misfolding, functional amyloid, and human disease,” Annu. Rev. Biochem. 75, 333–366 (2006).10.1146/annurev.biochem.75.101304.123901 - DOI - PubMed
    1. Serpell L. C., “Alzheimer’s amyloid fibrils: Structure and assembly,” Biochim. Biophys. Acta, Mol. Basis Dis. 1502, 16–30 (2000).10.1016/s0925-4439(00)00029-6 - DOI - PubMed
    1. Petkova A. T., Leapman R. D., Guo Z., Yau W.-M., Mattson M. P., and Tycko R., “Self-propagating, molecular-level polymorphism in Alzheimer’s β-amyloid fibrils,” Science 307, 262–265 (2005).10.1126/science.1105850 - DOI - PubMed
    1. Kodali R., Williams A. D., Chemuru S., and Wetzel R., “Aβ(1–40) forms five distinct amyloid structures whose β-sheet contents and fibril stabilities are correlated,” J. Mol. Biol. 401, 503–517 (2010).10.1016/j.jmb.2010.06.023 - DOI - PMC - PubMed
    1. Cohen M. L., Kim C., Haldiman T., ElHag M., Mehndiratta P., Pichet T., Lissemore F., Shea M., Cohen Y., Chen W., Blevins J., Appleby B. S., Surewicz K., Surewicz W. K., Sajatovic M., Tatsuoka C., Zhang S., Mayo P., Butkiewicz M., Haines J. L., Lerner A. J., and Safar J. G., “Rapidly progressive Alzheimer’s disease features distinct structures of amyloid-β,” Brain 138, 1009–1022 (2015).10.1093/brain/awv006 - DOI - PMC - PubMed

MeSH terms

LinkOut - more resources