Abstract
New nonfouling tubes are developed and their influence on the adhesion of neuroproteins is studied. The biomarkers are considered as single components (recombinant prion and Tau proteins) or in a solution of native and pathological forms. The samples are stored for 24 h at 4 °C in virgin and treated tubes layered with two different nanostructured coatings based on poly(N-isopropylacrylamide) with either a positive or a neutral charge, and the protein adhesion is monitored. The recombinant protein with a high pI is repelled from the nanostructured surface that has a negative ζ potential, whereas the recombinant protein with the lower pI is attracted. Furthermore, in the case of complex solutions, neutral nanostructured surfaces are able to retain all amyloid biomarkers.
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acrylamides / chemistry*
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Acrylic Resins
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Amyloid beta-Peptides / cerebrospinal fluid
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Amyloid beta-Peptides / chemistry*
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Coated Materials, Biocompatible / chemistry*
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Enzyme-Linked Immunosorbent Assay
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Humans
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Nanostructures
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Peptide Fragments / cerebrospinal fluid
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Peptide Fragments / chemistry*
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Photoelectron Spectroscopy
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Polymers / chemistry*
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Prions / cerebrospinal fluid
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Prions / chemistry*
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Protein Binding
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Recombinant Proteins / chemistry
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Solutions
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Static Electricity
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Surface Properties
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Thermodynamics
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tau Proteins / cerebrospinal fluid
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tau Proteins / chemistry*
Substances
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Acrylamides
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Acrylic Resins
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Amyloid beta-Peptides
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Coated Materials, Biocompatible
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Peptide Fragments
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Polymers
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Prions
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Recombinant Proteins
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Solutions
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amyloid beta-protein (1-42)
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tau Proteins
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poly-N-isopropylacrylamide