4.7 Article

An electrochemical peptide sensor for detection of dengue fever biomarker NS1

期刊

ANALYTICA CHIMICA ACTA
卷 1026, 期 -, 页码 109-116

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.aca.2018.04.005

关键词

Dengue virus; Early diagnosis; Affinity peptide; Electrochemical detection; Biosensor

资金

  1. National Research Foundation of Korea grant - Korea government (MSIP) [NRF-2014R1A2A2A01005621, NRF-2017R1A2A2A05001037]
  2. Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Science, ICT & Future Planning (MSIP) [NRF-2017R1A2B4009581]

向作者/读者索取更多资源

Dengue virus type 2 NS1 (DENV2 NS1) is a specific and sensitive protein biomarker for dengue fever diagnosis. In this study we used polyvalent phage display to identify unique affinity peptides that can bind NS1 protein. Cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS) were used to investigate the binding interactions. The potential affinity peptide-displayed phage from these methods was selected; its sequence was EHDRMHAYYLTR (R3#10). Amino acid sequence analysis showed that the peptide was rich in basic residues (two His and Arg). Among all the peptides tested, R3#10 showed the greatest decrease in current in CV and increase in impedance in EIS upon binding to NS1 proteins. EIS revealed that R3#10 phage clones were more specific towards NS1 proteins, as compared to bovine serum albumin or the M13 wild type used as control. Detection of NS1 proteins is in accordance with the electron-transfer resistance (Rct) value of the sensor layer, which is confirmed by EIS, and the Kd value of the R3# 10 peptide while binding to the phage particles was measured. To the best of our knowledge, this is the first example of identification and characterization of NS1 binding affinity peptides using phage display technology and electrochemical methods. We concluded that these new peptide-displayed phages or free peptides from phages may have potential applications in dengue diagnosis. (c) 2018 Elsevier B.V. All rights reserved.

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