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Far-Off Resonance: Multiwavelength Raman Spectroscopy Probing Amide Bands of Amyloid-β-(37–42) Peptide

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Department of Bioelectrochemistry and Biospectroscopy, Institute of Biochemistry, Life Sciences Center, Vilnius University, Saulėtekis Ave. 7, LT-10257 Vilnius, Lithuania
2
Department of Organic Chemistry, Center for Physical Sciences and Technology (FTMC), Saulėtekis Ave. 3, LT-10257 Vilnius, Lithuania
3
Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekis Ave. 7, LT-10257 Vilnius, Lithuania
*
Author to whom correspondence should be addressed.
Academic Editors: Paola Taddei and Michele Di Foggia
Molecules 2020, 25(15), 3556; https://doi.org/10.3390/molecules25153556
Received: 3 July 2020 / Revised: 24 July 2020 / Accepted: 2 August 2020 / Published: 4 August 2020
Several neurodegenerative diseases, like Alzheimer’s and Parkinson’s are linked with protein aggregation into amyloid fibrils. Conformational changes of native protein into the β-sheet structure are associated with a significant change in the vibrational spectrum. This is especially true for amide bands which are inherently sensitive to the secondary structure of a protein. Raman amide bands are greatly intensified under resonance conditions, in the UV spectral range, allowing for the selective probing of the peptide backbone. In this work, we examine parallel β-sheet forming GGVVIA, the C-terminus segment of amyloid-β peptide, using UV–Vis, FTIR, and multiwavelength Raman spectroscopy. We find that amide bands are enhanced far from the expected UV range, i.e., at 442 nm. A reasonable two-fold relative intensity increase is observed for amide II mode (normalized according to the δCH2/δCH3 vibration) while comparing 442 and 633 nm excitations; an increase in relative intensity of other amide bands was also visible. The observed relative intensification of amide II, amide S, and amide III modes in the Raman spectrum recorded at 442 nm comparing with longer wavelength (633/785/830 nm) excited spectra allows unambiguous identification of amide bands in the complex Raman spectra of peptides and proteins containing the β-sheet structure. View Full-Text
Keywords: amyloid fibril; protein aggregation; secondary structure; β-sheet; amide II; Raman spectroscopy amyloid fibril; protein aggregation; secondary structure; β-sheet; amide II; Raman spectroscopy
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MDPI and ACS Style

Talaikis, M.; Strazdaitė, S.; Žiaunys, M.; Niaura, G. Far-Off Resonance: Multiwavelength Raman Spectroscopy Probing Amide Bands of Amyloid-β-(37–42) Peptide. Molecules 2020, 25, 3556. https://doi.org/10.3390/molecules25153556

AMA Style

Talaikis M, Strazdaitė S, Žiaunys M, Niaura G. Far-Off Resonance: Multiwavelength Raman Spectroscopy Probing Amide Bands of Amyloid-β-(37–42) Peptide. Molecules. 2020; 25(15):3556. https://doi.org/10.3390/molecules25153556

Chicago/Turabian Style

Talaikis, Martynas; Strazdaitė, Simona; Žiaunys, Mantas; Niaura, Gediminas. 2020. "Far-Off Resonance: Multiwavelength Raman Spectroscopy Probing Amide Bands of Amyloid-β-(37–42) Peptide" Molecules 25, no. 15: 3556. https://doi.org/10.3390/molecules25153556

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