Life Science
High resolution imaging of protein structures
Time-resolved imaging of amyloid structures in living tissue at submicron resolution
(A-C) Single-frequency O-PTIR maps of the same spot in living brain tissue at time 0 and time 10 min.
(A) Change of β-sheet structure distribution over time, calculated as a ratio of 1630 cm–1 (the main β-sheet band) to 1656 cm–1 signal (Amide I maximum). Lower panel, white arrows indicate newly formed β-sheet structures.
(B) Change of distribution of fibrillar β-sheet structures over time, calculated as a ratio of 1680 cm–1 (antiparallel β-sheets) to 1656 cm–1 intensity. Lower panel, white arrows indicate newly formed antiparallel β-sheets.
(C) Change in lipid oxidation over time, calculated as a ratio of 1740 cm–1 (R-CO-OR groups) to 1656 cm–1 intensity. Lower panel, white arrows indicate new spots of lipid oxidation. (D) Overlay of (A-C) single-frequency IR maps, white arrows indicate colocalization of newly formed antiparallel β-sheets and oxidized lipids. The scale bar is the same for (A-D).
J. Am. Chem. Soc. 2023, 145, 45, 24796–24808. Open Access
Protein specific imaging with O-PTIR and co-located Fluorescence microscopy
Imaging amyloid plaques in brain tissue by FL-OPTIR.
(a) Fluorescent image of brain tissue with amyloid plaques labeled with Amytracker S20, overview.
(b) Zoom on to the amyloid plaque stained with Amytracker.
(c) O-PTIR Map demonstrating the distribution of β-sheet structures as a ratio of the bands at 1630–1656 cm⁻¹ in the plaque shown in panel (b).
(d) Averaged and normalized FL-OPTIR spectra were recorded from the outside, core, and plaque corona; the spectra locations were indicated by the markers of the corresponding color on the inset.
(e) Comparison of representative IR spectra on brain tissue (black) and Amytracker fluorescent dye (red). Error bars in panels (d) and (e) represent standard deviation.
New Insights into β-Sheet Structures and Carotenoid Associations in Alzheimer’s Disease
Amyloid β (Aβ) aggregation drives Alzheimer’s disease, yet understanding the chemistry of amyloid plaques remains challenging. This study uses Raman microspectroscopy to identify carotenoids in plaques and reveal their correlation with β-sheet-rich protein structures.
Optical photothermal infrared (O-PTIR) spectroscopy confirms these findings, showing elevated β-sheets in carotenoid-containing plaques but not in noncarotenoid plaques. These results suggest a link between anti-inflammatory carotenoids and specific secondary structural motifs in Aβ plaques, highlighting their potential role in neuroinflammation.
The study provides new insights into chemically distinct plaques and may inform therapeutic strategies for Alzheimer’s disease.
Webinars
- Life Science
Alzheimer’s Disease Research with Sub-micron Simultaneous IR+Raman: Co-localization of Beta-Sheets and Carotenoids in Aggregates
- October 30, 2024
- Life Science
Life science applications using novel submicron simultaneous IR and Raman microscopy – A new paradigm in vibrational spectroscopy
- October 3, 2019
- Life Science
Amyloid aggregates in neurons – Life science applications using submicron simultaneous IR and Raman microscopy
- March 26, 2020
- Life Science
Collagen orientation, fiber to submicron fibril life science applications of O-PTIR, from tissues to single cells and bacteria
- January 22, 2021
- Life Science
Single and intra-cell bacterial IR spectroscopy
- March 10, 2021
- Life Science
Live single cell analysis with simultaneous submicron IR+Raman spectroscopy
- April 29, 2021
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