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Electrochemical Sensing of Ovalbumin Based on the Interaction between Lysozyme Origin/Tyrosine‐rich Peptides Modified on Magnetic Beads and Oligothreonine/Ovalbumin‐origin Peptide
Author(s) -
Sugawara Kazuharu,
Ishizaki Sora,
Kuramitz Hideki,
Kadoya Toshihiko
Publication year - 2020
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.201900336
Subject(s) - ovalbumin , peptide , lysozyme , chemistry , tyrosine , electrochemistry , electron transfer , biophysics , combinatorial chemistry , antigen , biochemistry , photochemistry , electrode , biology , immunology
We developed a highly sensitive electrochemical system for the sensing of ovalbumin (OVA). Lysozyme origin/tyrosine‐rich peptides (RNRCKGTDVQAWY 4 C) were immobilized on magnetic beads, and the competitive reaction between OVA and oligothreonine/OVA origin peptide probe (T 8 VLLPDEVSG) could then be measured. In a previous study, the detection of OVA at the 10 −13 M level was achieved using RNRCKGTDVQAWY 4 C‐modified beads via a cross‐linker. To improve the sensitivity to OVA, this system uses T 8 VLLPDEVSG peptide probe to measure the interaction to RNRCKGTDVQAWY 4 C immobilized on magnetic beads. The peak of Y 4 C actually was an electron‐transfer peptide, which represented the oxidation of a phenolic hydroxyl group. First, we confirmed that the oxidation response of Y 4 C was increased based on an improvement in the electron transfer accessibility by oligothreonine. Next, T 8 VLLPDEVSG peptide probe was used for the electrochemical sensing of OVA in solutions that contained consistent amounts of RNRCKGTDVQAWY 4 C on magnetic beads. As a result, the peak current decreased as the concentration of OVA increased. The sensitivity to OVA was improved compared with the use of only RNRCKGTDVQAWY 4 C on magnetic beads. The OVA detection level was 10 −14 M, which approximates the results from antibody‐antigen reactions. Consequently, the proposed system is a powerful new concept in protein sensing.