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Frederik Franz Georg Fleissner

    Intracellular protein conformation measured with coherent Raman microspectroscopy
    • 2018

      Rheology experiments assess the bulk properties of materials, typically assuming sample homogeneity. However, this assumption is oversimplified for fibrin hydrogels and likely for other biopolymer networks. A key factor in measuring a sample's response to deformation is the precise application of stress. In cases where load distribution is significant, such as in hydrogel networks or extracellular matrix studies, traditional shear and tensile geometries may be inadequate. For microspectroscopy of fibrin and similar hydrogels, I propose an experimental setup: prepare a thin sample by casting between glass slides, embedding a small-diameter fiber (less than 100 μm) with greater elasticity than the test material during polymerization. This fiber will serve as a nucleation site for biopolymer formation, coupling it to the protein gel. Options for the fiber include stripped optical fibers, nanowires, or hair. The fiber's loose end can be attached to a micro stage or stepper motor while the hydrogel is fixed. Pulling on the fiber generates a controlled one-dimensional shear force, creating a specific stress distribution. This setup simulates physiological scenarios, such as deformation at a wound site by platelets or shear forces from blood flow. Local deformation can be monitored using embedded microbeads, particularly as shear strain exhibits a lateral gradient. It would be valuable to explore the relationship between shear force

      Intracellular protein conformation measured with coherent Raman microspectroscopy