Myosin VIIB Inhibitors

Myosin VIIB Inhibitors encompasses a variety of compounds that can directly or indirectly modulate the function of myosin VIIB, a crucial actin-based motor protein. Among these inhibitors, Blebbistatin is particularly notable for its ability to inhibit myosin II ATPase activity, a critical component of actomyosin contractility. Similarly, ML-7 and ML-9 are compounds that target the myosin light chain kinase, a pivotal regulator of myosin ATPase activity. By inhibiting this kinase, these compounds can decrease the ATPase activity of myosin, affecting its function.

Actin dynamics play a crucial role in determining the activity and functionality of myosin. This interplay is evident when observing the effects of compounds like SMIFH2, CK-636, Swinholide A, Jasplakinolide, and Cytochalasin D. While SMIFH2 inhibits formin, impacting actin polymerization, CK-636 acts on the Arp2/3 complex, another key component in actin dynamics. Swinholide A, Jasplakinolide, and Cytochalasin D have distinct roles in either disrupting, stabilizing, or inhibiting actin filaments and polymerization, respectively. Their influence on actin dynamics indirectly affects the function of myosins by modulating the primary substrate myosin acts upon. Additionally, compounds like Y-27632 and H-1152P inhibit ROCK, a kinase which influences myosin activity via phosphorylation of its light chain.