Publication date: 25th July 2016
Intermediate filaments are part of the cytoskeleton that serve a critical function in cellular load bearing at large deformations. The constituent proteins in these filaments have a defined secondary structure that is predicted to change under tensile loads. Our goal is to measure spatially-resolved protein secondary structure of mechanosensitive intermediate filaments in cells experiencing tensile and compressive loads. Using hyperspectral vibrational microscopy, we have successfully investigated the mechanically-induced secondary structural transition in fibrin as an in vitro model system with sub-micron spatial resolution. The α-helix, β-sheet, and random coil content at each position was calculated from spectral analysis of the amide I region of the Raman spectrum, which is sensitive to subtle changes in protein structure. Our results show load bearing in the fibrin gel, depicted by the secondary structure of the fibrin, is inhomogeneous with portions of the gel exhibiting no strain while other exhibit substantial strain. In this work, we present our first measurements of intracellular vimentin secondary structure in living cells. From this proof-of-concept, we will measure how the secondary structure vimentin changes under well-defined loads. This will allow to us to directly determine how intracellular protein structure of a load-bearing part of the cytoskeleton changes in response to mechanical loads.
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