The study presents a novel strategy for obtaining highly ordered interpolymeric complexes based on a protein, bovine serum albumin and a synthetic polymer, poly(aspartic acid). In this approach, experimental tests were carried out in the presence of a magnetic field of different intensities, namely 0.11 T and 0.3 T produced by permanent magnets. The influence of the magnetic force on the complexation process and the resulted self-assembled structures were studied by means of FTIR spectroscopy, X-ray diffraction, DLS, SEM microscopy and in vitro assay. The changes in the FTIR spectra acquired after 24 h of exposure were connected with conformational changes in the secondary structure and increased interactions between polymers, particularly when a higher intensity field was used. Due to a large anisotropy of magnetic susceptibility characteristic to both proteins and polypeptides, the magnetic field generated ordered assemblies consisting in globular structures of nanometric dimensions. This assembly strategy using magnets, along with remote manipulation capability can provide a versatile, contact-free, and inexpensive tool to create new, complex materials with tailorable characteristics.
Keywords: Bovine serum albumin; Interpolymeric complex; Magnetic field; Poly(aspartic acid).
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