Differentiation of protein secondary structure in clear and opaque human lenses: AFM – IR studies

Quantitative Chemical Analysis at the Nanoscale Using the Photothermal Induced Resonance Technique

“…29 Furthermore, while s-SNOM and PIFM are primarily surface sensitive techniques, PTIR probes samples thicknesses even in excess of 1 μm. 17,27 PTIR is finding ever growing applications in polymer science, 28,30,31 plasmonics, 32–35 photovoltaics, 11,25,36 pharmaceutics, 37 biology 14,38,39 and medicine 14 etc.…”

Atomic force microscopy of food assembly: Structural and mechanical insights at the nanoscale and potential opportunities from other fields

“…Protein fibers or fibrillation have been observed, e.g., in cytoskeleton or other structures using coupled AFM and super-resolution optical microscopies (Chacko, Zanacchi, & Diaspro, 2013;Cosentino, Canale, Bianchini, & Diaspro, 2019;Janel, Werkmeister, Bongiovanni, Lafont, & Barois, 2017), coupled AFM and total internal reflection fluorescence microscopy (TIRFM -Fukuda et al, 2013) or using coupled AFM and transmission electron microscopy (TEM - Yamada, Konno, & Shimabukuro, 2017). Protein identification or structures were investigated using coupled AFM and infrared spectroscopy (Ji et al, 2019;Paluszkiewicz et al, 2017) or using coupled AFM and mass spectroscopy using heated cantilevers (Andrade, Silva, Azevedo, Cunha, & Sousa, 2006;de Vries, 2015;Somnath, Jesse, Van Berkel, Kalinin, & Ovchinnikova, 2016). Coupling AFM with epifluorescence or with either surface-or tip-enhanced Raman spectroscopy has opened perspectives for the molecular recognition of polar lipids and inserted molecules such as cholesterol or peptides in supported bilayers (Bhatia et al, 2014;Opilik, Bauer, Schmid, Stadler, & Zenobi, 2011;Sweetenham, Larraona-Puy, & Notingher, 2011;Treffer et al, 2012).…”

Spectroscopic Imaging at the Nanoscale: Technologies and Recent Applications

“…Paluszkiewicz et al investigated cataract development in the human lens with AFM-IR, in which disease development was associated with the secondary structure of proteins. 196 Ruggeri et al applied AFM-IR to study the misfolding and aggregation of the Josephin domain of ataxin-3, implicated in spinocerebellar ataxia-3. 198 Taking advantages of the high chemical sensitivity and spatial resolution of AFM-IR, they monitored the conversion of monomers into amyloid β-sheet aggregates and linked the stiffness of amyloid structures to their β-sheet content at molecular level.…”