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http://dx.doi.org/10.1103/PhysRevLett.61.492 | DOI Listing |
Biomed Opt Express
December 2024
MOE Frontier Science Center for Brain Science & Brain-Machine Integration of Zhejiang University, Hangzhou 310027, China.
The crucial link between pathological protein aggregations and lipids in Alzheimer's disease pathogenesis is increasingly recognized, yet its spatial dynamics remain challenging for labeling-based microscopy. Here, we demonstrate photothermal ratio-metric infrared spectro-microscopy (PRISM) to investigate the structural and molecular compositions of pathological features in brain tissues at submicron resolution. By identifying the vibrational spectroscopic signatures of protein secondary structures and lipids, PRISM tracks the structural dynamics of pathological proteins, including amyloid and hyperphosphorylated Tau (pTau).
View Article and Find Full Text PDFMicrob Ecol
October 2024
GFZ German Research Centre for Geosciences, Potsdam, 14473, Telegrafenberg, Germany.
Nat Methods
October 2024
Department of Biostatistics and Center for Statistical Genetics, University of Michigan, Ann Arbor, MI, USA.
Int J Cosmet Sci
December 2024
SMIS Beamline, Synchrotron SOLEIL, L'Orme des Merisiers, Saint Aubin, France.
Objective: Today, there is only limited knowledge of the spatial organization of hair chemistry. Infrared microspectroscopy is a well-established tool to provide such information and has significantly contributed to this field. In this study, we present new results combining multiple infrared microspectroscopy methods at different length scales to create a better chemical histology of human hair, including the hair follicle, hair shaft, hair medulla and hair cuticle.
View Article and Find Full Text PDFMethods Enzymol
May 2024
Department of Chemistry and Biochemistry, The University of Alabama, Tuscaloosa, AL, United States. Electronic address:
The self-assembly of proteins and peptides into ordered structures called amyloid fibrils is a hallmark of numerous diseases, impacting the brain, heart, and other organs. The structure of amyloid aggregates is central to their function and thus has been extensively studied. However, the structural heterogeneities between aggregates as they evolve throughout the aggregation pathway are still not well understood.
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