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We study the high-frequency micro-mechanical response of suspensions composedby cardiac and skeletal muscle myosin by optical trapping interferometry. Weobserve that in low ionic strength solutions upon the addition of magnesiumadenosine triphosphate (\ch{MgATP^2-}), myosin suspensions radically changetheir micro-mechanics properties, generating a viscoelastic fluid characterizedby a complex modulus similar to a suspension of worm-like micelles. Thistransduction of energy, from chemical to mechanical, may be related to therelaxed states of myosin, which regulate muscle contractility and can beinvolved in the etiology of many myopathies. Within an analogous genericmechanical response, cardiac and skeletal myosin suspensions provide differentstress relaxation times, elastic modulus values, and characteristic lengths.These discrepancies probably rely on the dissimilar physiological functions ofcardiac and skeletal muscle, on the different MgATPase hydrolysis rates ofcardiac and skeletal myosins, and on the observed distinct cooperative behaviorof their myosin heads in the super-relaxed state. \textit{In vitro} studieslike these allow to understand the foundations of muscle cells mechanics on themicro-scale, and may contribute to the engineering of biological materialswhose micro-mechanics can be activated by energy regulators.

ATP-induced reconfiguration of the micro-viscoelasticity of cardiac and skeletal myosin solutions