Impedimetric biosensor fabricated with affinity peptides for sensitive detection of Escherichia coli O157:H7

Fan Shi; Lingfeng Gan; Yibing Wang; Ping Wang

doi:10.1007/s10529-020-02817-0

Impedimetric biosensor fabricated with affinity peptides for sensitive detection of Escherichia coli O157:H7

Fan Shi
, Lingfeng Gan
, Yibing Wang
, Ping Wang

Bioproducts and Biosystems Engineering

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

Objective: To effectively and conveniently detect pathogenic bacteria, this study aimed to develop label-free biosensors fabricated affinity peptides that can recognize targeted bacteria strains and enable precise quantitative detections. Results: A 12-mer peptide with high binding affinity toward Escherichia coli O157:H7 was discovered by biopanning of phage-displayed peptide library. The peptide modified with glycine residues (G₃) and one cysteine (C) residue at C-terminal, could self-assemble on gold electrodes, enabling electrochemical impedance spectroscopy (EIS) analysis for quantitative detection of E. coli O157:H7. This method showed a low detection limit of 20 CFU/mL and a liner range from 2 × 10² to 2 × 10⁶ CFU/mL. Conclusion: It appears that, by designing and optimizing the structures of peptides, such a strategy can be greatly promising in developing quick, sensitive and quantitative biosensor of pathogens.

Original language	English (US)
Pages (from-to)	825-832
Number of pages	8
Journal	Biotechnology Letters
Volume	42
Issue number	5
DOIs	https://doi.org/10.1007/s10529-020-02817-0
State	Published - May 1 2020

Bibliographical note

Funding Information:
This work was supported by the National Natural Science Foundation of China (Grant Nos.31471659, 21636003 and 21303050) and the Natural Science Foundation of Shanghai (Grant No.19ZR1412400).

Publisher Copyright:
© 2020, Springer Nature B.V.

Keywords

Affinity peptides
Biosensor
E. coli O157:H7
Electrochemical impedance spectroscopy

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10.1007/s10529-020-02817-0

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abstract = "Objective: To effectively and conveniently detect pathogenic bacteria, this study aimed to develop label-free biosensors fabricated affinity peptides that can recognize targeted bacteria strains and enable precise quantitative detections. Results: A 12-mer peptide with high binding affinity toward Escherichia coli O157:H7 was discovered by biopanning of phage-displayed peptide library. The peptide modified with glycine residues (G3) and one cysteine (C) residue at C-terminal, could self-assemble on gold electrodes, enabling electrochemical impedance spectroscopy (EIS) analysis for quantitative detection of E. coli O157:H7. This method showed a low detection limit of 20 CFU/mL and a liner range from 2 {\texttimes} 102 to 2 {\texttimes} 106 CFU/mL. Conclusion: It appears that, by designing and optimizing the structures of peptides, such a strategy can be greatly promising in developing quick, sensitive and quantitative biosensor of pathogens.",

keywords = "Affinity peptides, Biosensor, E. coli O157:H7, Electrochemical impedance spectroscopy",

author = "Fan Shi and Lingfeng Gan and Yibing Wang and Ping Wang",

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AU - Shi, Fan

AU - Gan, Lingfeng

AU - Wang, Yibing

AU - Wang, Ping

N1 - Funding Information: This work was supported by the National Natural Science Foundation of China (Grant Nos.31471659, 21636003 and 21303050) and the Natural Science Foundation of Shanghai (Grant No.19ZR1412400). Publisher Copyright: © 2020, Springer Nature B.V.

PY - 2020/5/1

Y1 - 2020/5/1

N2 - Objective: To effectively and conveniently detect pathogenic bacteria, this study aimed to develop label-free biosensors fabricated affinity peptides that can recognize targeted bacteria strains and enable precise quantitative detections. Results: A 12-mer peptide with high binding affinity toward Escherichia coli O157:H7 was discovered by biopanning of phage-displayed peptide library. The peptide modified with glycine residues (G3) and one cysteine (C) residue at C-terminal, could self-assemble on gold electrodes, enabling electrochemical impedance spectroscopy (EIS) analysis for quantitative detection of E. coli O157:H7. This method showed a low detection limit of 20 CFU/mL and a liner range from 2 × 102 to 2 × 106 CFU/mL. Conclusion: It appears that, by designing and optimizing the structures of peptides, such a strategy can be greatly promising in developing quick, sensitive and quantitative biosensor of pathogens.

AB - Objective: To effectively and conveniently detect pathogenic bacteria, this study aimed to develop label-free biosensors fabricated affinity peptides that can recognize targeted bacteria strains and enable precise quantitative detections. Results: A 12-mer peptide with high binding affinity toward Escherichia coli O157:H7 was discovered by biopanning of phage-displayed peptide library. The peptide modified with glycine residues (G3) and one cysteine (C) residue at C-terminal, could self-assemble on gold electrodes, enabling electrochemical impedance spectroscopy (EIS) analysis for quantitative detection of E. coli O157:H7. This method showed a low detection limit of 20 CFU/mL and a liner range from 2 × 102 to 2 × 106 CFU/mL. Conclusion: It appears that, by designing and optimizing the structures of peptides, such a strategy can be greatly promising in developing quick, sensitive and quantitative biosensor of pathogens.

KW - Affinity peptides

KW - Biosensor

KW - E. coli O157:H7

KW - Electrochemical impedance spectroscopy

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JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 5

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Impedimetric biosensor fabricated with affinity peptides for sensitive detection of Escherichia coli O157:H7

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