The adsorption and stability of model proteins onto polyelectrolyte multilayers prepared from naturally-derived polysaccharides was investigated. It was confirmed via FT-IR that both negatively- and positively-charged proteins adsorb onto both negatively-charged and neutral PEM. Both lysozyme and BSA undergo changes in their secondary structures when adsorbed to PEM, characterized by loss of α-helical content and increases in β-sheet structures. For lysozyme, the secondary structure is more stable when it is adsorbed from dilute solution. For BSA, the β-sheet structures that are formed during adsorption are apparently strongly H-bonded, as they undergo a reduced degree of HDX compared to the protein in solution.
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