Within the cytoskeleton, actin filaments are flexible structures that facilitate essential cellular functions such as movement and cell division. The organization and regulation of actin filaments and networks involve a variety of actin-binding proteins, one of which is palladin. Palladin plays a crucial role in regulating actin architecture in actively migrating cells and is often upregulated in response to more aggressive cancers, including breast and pancreatic cancers. However, the mechanisms through which palladin influences actin polymerization and filament bundling during cell migration are not fully understood. Experimental evidence from co-sedimentation assays suggests that palladin may affect both actin organization and the rate of polymerization. To investigate these effects, we employed Total Internal Reflection Fluorescence Microscopy (TIRFM) using in vitro purified proteins. By tracking individual filaments, we quantified the polymerization rates of actin under varying concentrations of both actin monomers and palladin. Our preliminary findings indicate that palladin enhances actin polymerization, which aligns with previous bulk measurements. For instance, one representative actin filament polymerized alone at a rate of approximately 0.048 µm/sec, while another actin strand in the presence of palladin polymerized at a rate of approximately 0.1342 µm/sec. Furthermore, TIRFM visualization revealed distinct differences in filament architecture. While actin alone formed primarily unbranched linear filaments, the addition of palladin promoted not only bundling but also the formation of highly branched, dendritic actin networks. These changes were accompanied by occasional bursts of filament elongation, suggesting that palladin may transiently accelerate polymerization and facilitate the assembly of higher-order structures. Our findings improve the understanding of how palladin modulates actin dynamics at the molecular level, particularly during the formation of complex filament architectures. Given palladin's known upregulation in aggressive cancers, its role in enhancing actin polymerization and bundling may contribute to the increased motility and invasiveness of cancer cells. This work lays the foundation for future studies exploring palladin as a potential therapeutic target in cytoskeletal regulation and cancer metastasis.