Preparation of S-sulfo albumin film and its cell adhesive property

Recently, large-scale production of the pharmaceutical grade recombinant human serum albumin was achieved, and several clinical trials have proved its safety and efficacy. Albumin is thought to be a candidate for a safe biopolymer sources for application to biomaterials. In this study, we treated albumin with sodium sulfite and sodium tetrathionate to give S-sulfo albumin, which was found to loose native albumin structure by CD spectra analysis and dye-binding assay. A water-insoluble S-sulfo albumin films were prepared by drying S-sulfo albumin solution and subsequent reformation of disulfide bonds by the oxidation with iodine. Ultimate strength, ultimate elongation and Young's modulus of S-sulfo albumin film prepared at room temperature were 3.3 ± 0.4 MPa, 30.8 ± 3.2% and 40.8 ± 3.3 MPa before oxidative treatment and changed to 13.8 ± 4.2 MPa, 5.6 ± 2.8% and 401.7 ± 15.3 MPa after oxidative treatment. When the film was prepared at 60 °C, similar tendency was observed. Thus, the disulfide bonds formation between albumin molecules by oxidative treatment converted the film stronger and stiffer. Cell adhesion and proliferation on the films were evaluated using mouse L929 fibroblast cells. Cell adhesion largely depended on the albumin structure; that is, cells did not attach to native albumin coated surfaces, while cell adhesion and proliferation occurred on the S-sulfo albumin films which lost their native albumin structure. Eighty percent of seeded cells were adhered on S-sulfo albumin films and proliferated well in a similar manner to those on the conventional culture dish. Our results indicate that S-sulfo albumin is a favorable cell culture substrate.