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Temperature-pH sensitivity of bovine serum albumin protein-microgels based on cross-linked poly(N-isopropylacrylamide-co-acrylic acid).

Abstract

Monodispersed poly(N-isopropylacrylamide-co-acrylic acid) (PNIPAM/AAc) microgels with various contents of acrylic acid (AAc) and cross-linker N,N'-methylenebisacrylamide (MBAAm) were synthesized by surfactant-free emulsion polymerization. The microgels exhibited affinity of binding bovine serum albumin (BSA) with increase of AAc contents. The adsorption amount of BSA was strongly dependent on suspension pH. The maximum adsorption was observed at around pH 4.0, while both low pH and basic conditions induced the rather low adsorption. In addition, AFM images showed that the microgel particles underwent bridging aggregation by loading BSA. The resultant BSA-microgel particles became more hydrophobic after loading BSA. Importantly, the adsorption of BSA onto PNIPAM/AAc microgel was found to alter the swelling/deswelling behavior of the resultant microgel suspensions. With the increase of BSA concentration, the volume phase transition temperature of BSA-microgel particles shifted to the lower temperature.

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  • Authors+Show Affiliations

    ,

    School of Materials Engineering, Zhengzhou University, Zhengzhou 450052 Henan, PR China. dxhuo@zzu.edu.cn

    , ,

    Source

    MeSH

    Acrylamides
    Acrylates
    Animals
    Cattle
    Gels
    Hot Temperature
    Hydrogen-Ion Concentration
    Microchemistry
    Microscopy, Atomic Force
    Molecular Structure
    Polymers
    Protein Binding
    Serum Albumin, Bovine
    Temperature

    Pub Type(s)

    Journal Article
    Research Support, Non-U.S. Gov't

    Language

    eng

    PubMed ID

    16698239