Changes in the structure and function of myofibrils during pressurization using a high-pressure microscope

When pressure is applied to a solution, the pressure is instantly and uniformly transmitted throughout the solution because the solution is incompressible. When this hydrostatic pressure is 40 to 80 MPa, the protein is not destroyed and the interaction between the hydrophilic / hydrophobic residues on the protein surface and the water molecule changes. As a result, the bonds between proteins can be weakened to promote structural changes such as depolymerization.

How myofibrils change structure and motor function under high hydrostatic pressure was measured in real time with a high-pressure microscope.

Video 1.

Structural changes in myofibrils when a pressure of 60 MPa was applied in relaxing solution.

The imaging speed at the time of measurement was 30 fps. The scale bar is 10 µm.

Video 2.

Structural changes in myofibrils when a pressure of 60 MPa was applied in rigor solution.

The imaging speed at the time of measurement was 1 fps. The scale bar is 10 µm.

Video 3.

Sarcomeric oscillation of myofibrils under 0.1 MPa pressure.

The imaging speed at the time of measurement was 30 fps. The scale bar is 10 µm.

Video 4.

Sarcomeric oscillation of myofibrils under 40 MPa pressure.

The imaging speed at the time of measurement was 30 fps. The scale bar is 10 µm.

Video 5.

Sarcomeric oscillation of myofibrils under 50 MPa pressure.

The imaging speed at the time of measurement was 30 fps. The scale bar is 10 µm.

Video 6.

Sarcomeric oscillation of myofibrils under a pressure of 0.1 MPa after pressure treatment.

The imaging speed at the time of measurement was 30 fps. The scale bar is 10 µm.

Video 7.

Structural changes in myofibrils when a pressure of 80 MPa was applied in rigor solution.

The imaging speed at the time of measurement was 1 fps.