title: Fourier Transform Infrared (FTIR) Spectroscopy, Ultraviolet Resonance Raman (UVRR) Spectroscopy, and Atomic Force Microscopy (AFM) for Study of the Kinetics of Formation and Structural Characterization of Tau Fibrils.
abstract: Kinetic studies of tau fibril formation in vitro most commonly employ spectroscopic probes such as thioflavinT fluorescence and laser light scattering or negative stain transmission electron microscopy. Here, I describe the use of Fourier transform infrared (FTIR) spectroscopy, ultraviolet resonance Raman (UVRR) spectroscopy, and atomic force microscopy (AFM) as complementary probes for studies of tau aggregation. The sensitivity of vibrational spectroscopic techniques (FTIR and UVRR) to secondary structure content allows for measurement of conformational changes that occur when the intrinsically disordered protein tau transforms into cross-β-core containing fibrils. AFM imaging serves as a gentle probe of structures populated over the time course of tau fibrillization. Together, these assays help further elucidate the structural and mechanistic complexity inherent in tau fibril formation.
authors.affiliation: Department of Molecular Biosciences, Northwestern University, 2205 Tech Drive, Hogan 2-100, Evanston, IL, 60208, USA. gayathri.1984@gmail.com.
authors.forename: Gayathri
authors.initials: G
authors.lastname: Ramachandran
mesh_terms: D000818:Animals; D006801:Humans; D007700:Kinetics; D018625:Microscopy, Atomic Force / Q000379:methods*; D066263:Protein Aggregation, Pathological / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*; D013059:Spectrum Analysis, Raman / Q000379:methods*; D016875:tau Proteins / Q000737:chemistry*
chemical_list: D016875:tau Proteins
keywords: AFM; Amyloid fibril; FTIR spectroscopy; Heparin; Kinetics; Neurodegeneration; Tau; UVRR spectroscopy