Bovine serum albumin and lysozyme nanofibers as versatile platforms for preserving loaded bioactive compounds

In this study, the electrospinning procedure was optimized to create polyethylene oxide (PEO) NFs highly enriched in proteins with non-structural functions while preserving their activity. For this purpose, several immune-related proteins of low, medium and high molecular weights were used as molecular models. Initially, the electrospinning parameters were adjusted using 3 % w/w PEO and bovine serum albumin (BSA, 5-20 % w/w). As determined by FESEM, their average diameters ranged from 301 to 752 nm, and those with higher protein content (15-20 %) yielded more uniform NFs in both size and morphology terms. Protein integrity remained stable as determined by SDS-PAGE and FTIR. Similar results were observed for the polypeptide lysozyme (LYZ) when incorporated in NFs under these settings. To further explore the potential of these materials, the antimicrobial peptide piscidin (PIS) and an antibody (Ab, HRP-IgG) were used to produce BSA/PIS, LYZ/PIS and BSA/Ab NFs and evaluate the preservation of their activity. The antibacterial assays showed that, in most bacterial species, the activity of PIS remained consistent after being incorporated into the NFs. Furthermore, the activity of HRP-IgG was maintained within the NFs, with enhanced preservation observed in BSA/Ab NFs. These findings expand the possibilities of protein utilization across various applications through nanomaterials.