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  • Title: Interactions between bovine serum albumin and Langmuir films composed of charged and uncharged poly(N-isopropylacrylamide) block copolymers.
    Author: Volden S, Ese MH, Zhu K, Yasuda M, Nyström B, Glomm WR.
    Journal: Colloids Surf B Biointerfaces; 2012 Oct 01; 98():50-7. PubMed ID: 22652359.
    Abstract:
    The thermoresponsive poly(N-isopropylacrylamide) (PNIPAAM) and NIPAAM block copolymer derivatives are attractive for drug delivery applications as they contract reversibly at lower critical solution temperatures (LCST) close to physiological conditions. In order to investigate biomaterial-protein compatibility, we have studied the interaction between PNIPAAM copolymer films spread at the air-water surface and bovine serum albumin (BSA) injected below the precompressed polymer films, using the Langmuir technique coupled with Brewster angle microscopy (BAM). A PNIPAAM homopolymer was applied together with a number of PNIPAAM-based di- and triblock copolymers, to assess effects of e.g., charge and hydrophobicity on protein-polymer interactions. The nature and strength of protein-polymer interaction was found to be tunable, ranging from complex formation (PNIPAAM homopolymer) to mixed monolayers and electrostatic cross-linking, according to the nature of the co-monomer. Results show that intercalation versus adsorption can be controlled through polymer composition.
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