Printing biomacromolecules on a bovine serum albumin precursor layer

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Abstract

Various biomacromolecules including proteins and polysaccharides are printed on a substrate capped with a bovine serum albumin (BSA) precursor layer to create clear co-patterns of these molecules. Characterizations by confocal laser scanning microscopy (CLSM) and atomic force microscopy (AFM) demonstrate the successful production and clear boundaries of the co-patterns. Rinsing the BSA-adsorbed substrate and the biomacromolecules-inked stamp before microcontact printing (μCP) is crucial for the creation of clear and stable co-patterns. The patterns are mainly stabilized by electrostatic interactions and van der Waals forces. Characterizations by ellipsometry, UV-Vis and fluorescence spectroscopy reveal that printing by a flat PDMS stamp yields a denser layered structure of proteins with a higher amount than that of adsorbed proteins. By printing, however, a lower enzymatic catalytic activity for horseradish peroxidase (HRP) or binding capability for avidin (both normalized to amount) is determined. A conformational transition from α-helix to β-sheet of HRP is observed by ATR-IR. By contrast, a BSA precursor layer can effectively improve the functionality of the printed HRP or avidin and preserve the original confermation of the proteins, although the absolute transferred amount of these proteins is decreased. © 2005 WILEY-VCH Verlag GmbH & Co. KGaA.

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Wang, B., Feng, J., & Gao, C. (2005). Printing biomacromolecules on a bovine serum albumin precursor layer. Macromolecular Bioscience, 5(8), 767–774. https://doi.org/10.1002/mabi.200500037

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