Sarcomeric control proteins

Figure 6.69. A biomimetic approach toward skeletal muscle movement. Shown is (a) the stacked protein filaments of the sarcomere and (b) a redox-controlled molecular analogue. Adapted with permission from Liu, Y. Flood, A. H. Bonvallet, P. A. Vignon, S. A. Northrop, B. H. Tseng, H.-R. Jeppesen, J. O. Huang, T. J. Brough, B. Bailer, M. Magonov, S. Solares, S. D. Goddard, W. A. Ho, C.-M. Stoddart, J. F. J. Am. Chem. Soc. 2005, 727, 9745. Copyright 2005 American Chemical Society.

The cellular unit that is active toward the contraction of skeletal muscles, known as the sarcomere, is comprised of alternatively stacked filaments of the proteins actin and myosin. During muscle contraction, the protein filaments slide past each other as a result of a rowing action of the surface myosin heads (Figure 6.92a). Hence, an effective biomimetic approach would entail the design of a linear architecture that features sliding components that will respond to a chemical stimulus. This approach has recently been demonstrated with the design of a rotaxane molecule that exhibits redox-controlled contraction and extension of the molecular architecture, in response to a chemical or electrochemical stimulus (Figure 6.92b). ... 

Since VCP has been well characterized to indirectly control sarcomere organization by regulating the cellular levels of Unc-45 during muscle fiber development [37], we quantified Unc-45 protein levels in muscle tissue lysates from wild-type and mutant VCP mice. Unc-45 protein levels were found to be... 

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