In this paper, the development of a new affinity carrier was the key point for the
anti-amyloid ß 1–42 antibodies detection in human serum, as the potential marker of
the Alzheimer’s disease. Magnetic solid-phase preparation comprised the amyloid
ß 1–42 peptide immobilization on the superparamagnetic carboxyl beads that had been
modified by bisamino-polyethylene glycol spacer to gain terminal amine groups and
subsequently analyzed by the zeta potential measurement. The following immobilization
of the amyloid ß 1–42 peptide onto the modified superparamagnetic beads was
performed by the carbodiimide chemistry. Nonspecific sorption of serum contaminants
was prevented by using of bovine serum albumin. The developed magnetic carrier was
analyzed by scanning electron microscopy. The amyloid ß 1–42 peptide bioaffinity
carrier was applied for detection of natural anti-amyloid ß 1–42 antibodies in human
serum. A comparison with spacer-free bioaffinity carrier has confirmed a divergent
optical density values for control serum sample. The new bioaffinity carrier was applied
to the detection of anti-amyloid ß 1–42 antibodies in control serum and in sera of
patients with neurodegenerative disorders.
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dc.format
p. 41 - 52
dc.language.iso
en
dc.publisher
University of Pardubice
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dc.relation.ispartof
Scientific papers of the University of Pardubice. Series A, Faculty of Chemical Technology. 25/2019
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dc.rights
open access
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dc.subject
anti-amyloid ß 1–42
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dc.subject
magnetic bioaffinity carrier
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dc.subject
immobilization
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dc.title
Development of the magnetic bioaffinity carrier for the anti-amyloid beta 1–42 antibodies detection