Actin cytoskeleton reorganization plays essential roles in many cellular processes such as cell structure maintenance, cell motility, and force generation. Cytoskeletal drugs are small molecules that act on cytoskeletal components by either stabilizing or destabilizing them. Swinholide A is an actin-binding drug derived from the marine sponge. Swinholide A binds actin dimers as well as severs filaments. The main objective of this project is to determine how Swinholide A modulates actin filament assembly dynamics in the presence of macromolecular crowding. We utilize total internal reflection fluorescence (TIRF) microscopy imaging to directly visualize Swinholide A-mediated actin filament disassembly and severing. Filament disassembly and severing are evaluated by calculating actin filament lengths and length distribution controlled by Swinholide A. This study helps us better understand the fundamental mechanism by which Swinholide A affects actin assembly and disassembly dynamics. Further studies will allow for investigating new methods of treatment for a range of different diseases that have pathogenetically high levels of filamentous actin, such as cystic fibrosis, as well as a drug to combat the explosive expansion of cancers.