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Cubosomes are self-assembled lipid nanoparticles with potential for use as drug carriers. Their internal structure, composed of bicontinuous cubic phases, allows the encapsulation of hydrophilic, hydrophobic, and amphiphilic compounds within the same matrix. For systemic applications, understanding their interaction with plasma proteins is essential, as such interactions can modify the physicochemical properties of the nanoparticles, affecting colloidal stability, drug release rate, and biodistribution. Bovine Serum Albumin (BSA) was used as a model protein due to its relevance in binding and transporting molecules in plasma, making it important to assess whether its association with cubosomes induces structural or aggregation changes. The interaction between cubosomes and BSA was evaluated by dynamic light scattering (DLS) and circular dichroism (CD). DLS results indicated an increase in hydrodynamic diameter after incubation with BSA, suggesting complex formation. CD analysis showed that the secondary structure of the protein was relatively preserved. These results indicate that cubosomes form complexes with BSA without significant changes in the protein’s secondary structure, providing useful information for the design of drug delivery systems that consider nanoparticle–protein interactions at the planning stage to achieve greater predictability and therapeutic efficiency.
This work was supported by Fundação de Amparo à Pesquisa do Estado de São Paulo (processes 2017/26131–5 and 2022/02378–0) and CNPq (National Council for Scientific and Technological Development, process: 309418/2021–6).
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