Resumen:
endritic polyglycerol (PG) functionalized surfaces represent a good alternative for preparation of
protein resistant materials, whose versatility can be enhanced by conferring them the ability to bind
particular biomolecules of interest to the surface. In this work, PG derivatives bearing disulfide and
different loadings of amino moieties (0?14%) were synthesized and attached to gold surfaces. The
modified surfaces were characterized by means of infrared reflection adsorption spectroscopy
(FT-IRRAS), X-ray photoelectron spectroscopy (XPS), and contact angle measurements. The protein
resistance properties of the PG-modified surfaces were evaluated by surface plasmon resonance (SPR)
spectroscopy using fibrinogen, albumin, pepsin, and lysozyme as model proteins. The availability and
accessibility of the amino groups to bind biomolecules were assessed by fluorescence measurements.
This study demonstrates that PG-coated surfaces with amino contents up to 9% still show very good
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