Protein interactions with model chromatographic stationary phases constructed using self-assembled monolayers |
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Authors: | Barrett David A Power Gillian M Hussain Maruf A Pitfield Ian D Shaw P Nicholas Davies Martyn C |
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Institution: | School of Pharmacy, University of Nottingham, University Park, Nottingham NG7 2RD, UK. david.barrett@nottingham.ac.uk |
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Abstract: | Model surfaces representative of chromatographic stationary phases were developed by immobilising an homologous series (C2-C18) of n-alkylthiols, mixed monolayers of C4/C18 and thioalkanes with alcohol, carboxylic acid, amino and sulphonic acid terminal groups onto a flat, silver-coated glass surface using self-assembled monolayer (SAM) chemistry. The processes of adsorption and desorption of serum albumins onto the monolayer surfaces was monitored in real-time using surface plasmon resonance (SPR). Alkyl-terminated SAMs all showed a strong adsorption of bovine serum albumin which was largely independent of alkyl chain length, the ratio of mixed C4/C18 SAMs or the solution pH/ionic strength. The adsorption of human serum albumin to carboxylic and amine terminated SAMs was shown to be predominantly via non-electrostatic interactions (hydrophobic or hydrogen bonding). However, sulphonic acid terminated SAMs showed almost exclusively electrostatic interactions with human serum albumin. This preliminary work using self-assembled monolayer chemistry confirms the usefulness of well characterised SAMs surfaces for investigating protein adsorption and desorption onto/from model chromatography surfaces and gives some guidance for selecting appropriate functionalities to develop better surfaces for chromatography and electrophoresis. |
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Keywords: | Model surface Stationary phase Self‐assembled monolayer Surface plasmon resonance Serum albumin |
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