Fluorescently Guided Optical Photothermal Infrared Microspectroscopy for Protein-Specific Bioimaging at Subcellular Level
(2023) In Journal of Medicinal Chemistry 66(4). p.2542-2549- Abstract
Infrared spectroscopic imaging is widely used for the visualization of biomolecule structures, and techniques such as optical photothermal infrared (OPTIR) microspectroscopy can achieve <500 nm spatial resolution. However, these approaches lack specificity for particular cell types and cell components and thus cannot be used as a stand-alone technique to assess their properties. Here, we have developed a novel tool, fluorescently guided optical photothermal infrared microspectroscopy, that simultaneously exploits epifluorescence imaging and OPTIR to perform fluorescently guided IR spectroscopic analysis. This novel approach exceeds the diffraction limit of infrared microscopy and allows structural analysis of specific proteins... (More)
Infrared spectroscopic imaging is widely used for the visualization of biomolecule structures, and techniques such as optical photothermal infrared (OPTIR) microspectroscopy can achieve <500 nm spatial resolution. However, these approaches lack specificity for particular cell types and cell components and thus cannot be used as a stand-alone technique to assess their properties. Here, we have developed a novel tool, fluorescently guided optical photothermal infrared microspectroscopy, that simultaneously exploits epifluorescence imaging and OPTIR to perform fluorescently guided IR spectroscopic analysis. This novel approach exceeds the diffraction limit of infrared microscopy and allows structural analysis of specific proteins directly in tissue and single cells. Experiments described herein used epifluorescence to rapidly locate amyloid proteins in tissues or neuronal cultures, thus guiding OPTIR measurements to assess amyloid structures at the subcellular level. We believe that this new approach will be a valuable addition to infrared spectroscopy providing cellular specificity of measurements in complex systems for studies of structurally altered protein aggregates.
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- author
- Prater, Craig ; Bai, Yeran ; Konings, Sabine C LU ; Martinsson, Isak LU ; Swaminathan, Vinay S LU ; Nordenfelt, Pontus LU ; Gouras, Gunnar LU ; Borondics, Ferenc and Klementieva, Oxana LU
- organization
-
- Medical Microspectroscopy (research group)
- NanoLund: Centre for Nanoscience
- MultiPark: Multidisciplinary research focused on Parkinson´s disease
- Department Office of Experimental Medical Science
- Department of Experimental Medical Science
- LUCC: Lund University Cancer Centre
- WCMM-Wallenberg Centre for Molecular Medicine
- Department of Clinical Sciences, Malmö
- Experimental Dementia Research (research group)
- publishing date
- 2023-01-04
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Medicinal Chemistry
- volume
- 66
- issue
- 4
- pages
- 2542 - 2549
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:36599042
- scopus:85146027211
- ISSN
- 1520-4804
- DOI
- 10.1021/acs.jmedchem.2c01359
- language
- English
- LU publication?
- yes
- id
- 7766bb51-580b-4f30-bdff-98bac5315a5a
- date added to LUP
- 2023-02-03 04:41:09
- date last changed
- 2024-12-14 11:57:05
@article{7766bb51-580b-4f30-bdff-98bac5315a5a, abstract = {{<p>Infrared spectroscopic imaging is widely used for the visualization of biomolecule structures, and techniques such as optical photothermal infrared (OPTIR) microspectroscopy can achieve <500 nm spatial resolution. However, these approaches lack specificity for particular cell types and cell components and thus cannot be used as a stand-alone technique to assess their properties. Here, we have developed a novel tool, fluorescently guided optical photothermal infrared microspectroscopy, that simultaneously exploits epifluorescence imaging and OPTIR to perform fluorescently guided IR spectroscopic analysis. This novel approach exceeds the diffraction limit of infrared microscopy and allows structural analysis of specific proteins directly in tissue and single cells. Experiments described herein used epifluorescence to rapidly locate amyloid proteins in tissues or neuronal cultures, thus guiding OPTIR measurements to assess amyloid structures at the subcellular level. We believe that this new approach will be a valuable addition to infrared spectroscopy providing cellular specificity of measurements in complex systems for studies of structurally altered protein aggregates.</p>}}, author = {{Prater, Craig and Bai, Yeran and Konings, Sabine C and Martinsson, Isak and Swaminathan, Vinay S and Nordenfelt, Pontus and Gouras, Gunnar and Borondics, Ferenc and Klementieva, Oxana}}, issn = {{1520-4804}}, language = {{eng}}, month = {{01}}, number = {{4}}, pages = {{2542--2549}}, publisher = {{The American Chemical Society (ACS)}}, series = {{Journal of Medicinal Chemistry}}, title = {{Fluorescently Guided Optical Photothermal Infrared Microspectroscopy for Protein-Specific Bioimaging at Subcellular Level}}, url = {{http://dx.doi.org/10.1021/acs.jmedchem.2c01359}}, doi = {{10.1021/acs.jmedchem.2c01359}}, volume = {{66}}, year = {{2023}}, }