New PEPTIR-2.0 Peptide Designed for Use as Recognition Element in Electrochemical Biosensors with Improved Specificity towards <i>E. coli</i> O157:H7
The detection of pathogens through alternative methodologies based on electrochemical biosensors is being studied. These devices exhibit remarkable properties, such as simplicity, specificity, and high sensitivity in monitoring pathogens. However, it is necessary to continue conducting studies that...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2022-04-01
|
Series: | Molecules |
Subjects: | |
Online Access: | https://www.mdpi.com/1420-3049/27/9/2704 |
_version_ | 1797503770773422080 |
---|---|
author | Jose Luis Ropero-Vega Joshua Felipe Redondo-Ortega Juliana Paola Rodríguez-Caicedo Paola Rondón-Villarreal Johanna Marcela Flórez-Castillo |
author_facet | Jose Luis Ropero-Vega Joshua Felipe Redondo-Ortega Juliana Paola Rodríguez-Caicedo Paola Rondón-Villarreal Johanna Marcela Flórez-Castillo |
author_sort | Jose Luis Ropero-Vega |
collection | DOAJ |
description | The detection of pathogens through alternative methodologies based on electrochemical biosensors is being studied. These devices exhibit remarkable properties, such as simplicity, specificity, and high sensitivity in monitoring pathogens. However, it is necessary to continue conducting studies that adequately improve these characteristics, especially the recognition molecule. This work aims to design and evaluate a new peptide, named PEPTIR-2.0, as a recognition molecule in electrochemical biosensors to detect <i>E. coli</i> O157:H7 in water. PEPTIR-2.0 was obtained from modifications of the PEPTIR-1.0 peptide sequence, which was previously reported and exhibited excellent properties for detecting and quantifying this pathogenic microorganism. PEPTIR-1.0 is a peptide analogous to the TIR (Translocated Intimin Receptor) protein capable of interacting with the Intimin outer membrane. The basis of this study was to obtain, by using bioinformatics tools, a molecule analogous to PEPTIR-1.0 that maintains its three-dimensional structure but increases the hydrophobic interactions between it and Intimin, since these intermolecular forces are the predominant ones. The designed PEPTIR-2.0 peptide was immobilized on screen-printed electrodes modified with gold nanoparticles. The detection capacity of <i>E. coli</i> O157:H7 in water was evaluated using electrochemical impedance spectroscopy in the presence of other microorganisms, such as <i>P. aeruginosa</i>, <i>S. aureus</i>, and non-pathogenic <i>E. coli</i>. The results showed that PEPTIR-2.0 confers remarkable specificity to the biosensor towards detecting <i>E. coli</i>, even higher than PEPTIR-1.0. |
first_indexed | 2024-03-10T03:55:05Z |
format | Article |
id | doaj.art-df9bd2e3b94b44a780c85cd6e7fbf59c |
institution | Directory Open Access Journal |
issn | 1420-3049 |
language | English |
last_indexed | 2024-03-10T03:55:05Z |
publishDate | 2022-04-01 |
publisher | MDPI AG |
record_format | Article |
series | Molecules |
spelling | doaj.art-df9bd2e3b94b44a780c85cd6e7fbf59c2023-11-23T08:48:23ZengMDPI AGMolecules1420-30492022-04-01279270410.3390/molecules27092704New PEPTIR-2.0 Peptide Designed for Use as Recognition Element in Electrochemical Biosensors with Improved Specificity towards <i>E. coli</i> O157:H7Jose Luis Ropero-Vega0Joshua Felipe Redondo-Ortega1Juliana Paola Rodríguez-Caicedo2Paola Rondón-Villarreal3Johanna Marcela Flórez-Castillo4Universidad de Santander, Facultad de Ciencias Naturales, Ciencias Básicas y Aplicadas Para la Sostenibilidad—CIBAS, Calle 70 No. 55-210, Santander, Bucaramanga C.P. 680003, ColombiaUniversidad de Santander, Facultad de Ciencias Naturales, Ciencias Básicas y Aplicadas Para la Sostenibilidad—CIBAS, Calle 70 No. 55-210, Santander, Bucaramanga C.P. 680003, ColombiaUniversidad de Santander, Facultad de Ciencias Naturales, Ciencias Básicas y Aplicadas Para la Sostenibilidad—CIBAS, Calle 70 No. 55-210, Santander, Bucaramanga C.P. 680003, ColombiaUniversidad de Santander, Facultad de Ciencias Médicas y de la Salud, Instituto de Investigación Masira, Calle 70 No. 55-210, Santander, Bucaramanga C.P. 680003, ColombiaUniversidad de Santander, Facultad de Ciencias Naturales, Ciencias Básicas y Aplicadas Para la Sostenibilidad—CIBAS, Calle 70 No. 55-210, Santander, Bucaramanga C.P. 680003, ColombiaThe detection of pathogens through alternative methodologies based on electrochemical biosensors is being studied. These devices exhibit remarkable properties, such as simplicity, specificity, and high sensitivity in monitoring pathogens. However, it is necessary to continue conducting studies that adequately improve these characteristics, especially the recognition molecule. This work aims to design and evaluate a new peptide, named PEPTIR-2.0, as a recognition molecule in electrochemical biosensors to detect <i>E. coli</i> O157:H7 in water. PEPTIR-2.0 was obtained from modifications of the PEPTIR-1.0 peptide sequence, which was previously reported and exhibited excellent properties for detecting and quantifying this pathogenic microorganism. PEPTIR-1.0 is a peptide analogous to the TIR (Translocated Intimin Receptor) protein capable of interacting with the Intimin outer membrane. The basis of this study was to obtain, by using bioinformatics tools, a molecule analogous to PEPTIR-1.0 that maintains its three-dimensional structure but increases the hydrophobic interactions between it and Intimin, since these intermolecular forces are the predominant ones. The designed PEPTIR-2.0 peptide was immobilized on screen-printed electrodes modified with gold nanoparticles. The detection capacity of <i>E. coli</i> O157:H7 in water was evaluated using electrochemical impedance spectroscopy in the presence of other microorganisms, such as <i>P. aeruginosa</i>, <i>S. aureus</i>, and non-pathogenic <i>E. coli</i>. The results showed that PEPTIR-2.0 confers remarkable specificity to the biosensor towards detecting <i>E. coli</i>, even higher than PEPTIR-1.0.https://www.mdpi.com/1420-3049/27/9/2704PEPTIR-1.0bioinformatics toolspathogenwaterelectrochemical impedance spectroscopyhigh specificity |
spellingShingle | Jose Luis Ropero-Vega Joshua Felipe Redondo-Ortega Juliana Paola Rodríguez-Caicedo Paola Rondón-Villarreal Johanna Marcela Flórez-Castillo New PEPTIR-2.0 Peptide Designed for Use as Recognition Element in Electrochemical Biosensors with Improved Specificity towards <i>E. coli</i> O157:H7 Molecules PEPTIR-1.0 bioinformatics tools pathogen water electrochemical impedance spectroscopy high specificity |
title | New PEPTIR-2.0 Peptide Designed for Use as Recognition Element in Electrochemical Biosensors with Improved Specificity towards <i>E. coli</i> O157:H7 |
title_full | New PEPTIR-2.0 Peptide Designed for Use as Recognition Element in Electrochemical Biosensors with Improved Specificity towards <i>E. coli</i> O157:H7 |
title_fullStr | New PEPTIR-2.0 Peptide Designed for Use as Recognition Element in Electrochemical Biosensors with Improved Specificity towards <i>E. coli</i> O157:H7 |
title_full_unstemmed | New PEPTIR-2.0 Peptide Designed for Use as Recognition Element in Electrochemical Biosensors with Improved Specificity towards <i>E. coli</i> O157:H7 |
title_short | New PEPTIR-2.0 Peptide Designed for Use as Recognition Element in Electrochemical Biosensors with Improved Specificity towards <i>E. coli</i> O157:H7 |
title_sort | new peptir 2 0 peptide designed for use as recognition element in electrochemical biosensors with improved specificity towards i e coli i o157 h7 |
topic | PEPTIR-1.0 bioinformatics tools pathogen water electrochemical impedance spectroscopy high specificity |
url | https://www.mdpi.com/1420-3049/27/9/2704 |
work_keys_str_mv | AT joseluisroperovega newpeptir20peptidedesignedforuseasrecognitionelementinelectrochemicalbiosensorswithimprovedspecificitytowardsiecoliio157h7 AT joshuafeliperedondoortega newpeptir20peptidedesignedforuseasrecognitionelementinelectrochemicalbiosensorswithimprovedspecificitytowardsiecoliio157h7 AT julianapaolarodriguezcaicedo newpeptir20peptidedesignedforuseasrecognitionelementinelectrochemicalbiosensorswithimprovedspecificitytowardsiecoliio157h7 AT paolarondonvillarreal newpeptir20peptidedesignedforuseasrecognitionelementinelectrochemicalbiosensorswithimprovedspecificitytowardsiecoliio157h7 AT johannamarcelaflorezcastillo newpeptir20peptidedesignedforuseasrecognitionelementinelectrochemicalbiosensorswithimprovedspecificitytowardsiecoliio157h7 |