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Myosin Modulator Aficamten Inhibits Force by Altering Myosin's Biochemical Activity Without Changing Thick Filament Structure
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DOI：10.1016/j.jacbts.2025.101449.png)
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Abstract
En 中文
We investigated the effects of aficamten on cardiac muscle structure, biochemical activity, and contractile function. Aficamten does not structurally sequester myosin heads along the thick filament. It inhibits ATPase activity by decreasing myosin ATPase cycling kinetics, with the emergence of a super slow biochemical nucleotide turnover. This results in decreased force and calcium sensitivity without altering cross-bridge cycling. Our myofibril mechanical assay showed inhibition of force with accelerated relaxation. In engineered heart tissues, while mavacamten and aficamten inhibit cardiac twitch forces, mavacamten reduces the activation kinetics while both accelerate relaxation. (JACC Basic Transl Sci. 2026;11:101449) (c) 2026 The Authors. Published by Elsevier on behalf of the American College of Cardiology Foundation. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
Keywords:
HYPERTROPHIC CARDIOMYOPATHY
MAVACAMTEN
LENGTH
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