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Engineered synthetic nanobody-based biosensors for electrochemical detection of epidermal growth factor receptor
dc.contributor.author | Cruz-Pacheco A.F | |
dc.contributor.author | Monsalve Y | |
dc.contributor.author | Serrano-Rivero Y | |
dc.contributor.author | Salazar-Uribe J | |
dc.contributor.author | Moreno E | |
dc.contributor.author | Orozco J. | |
dc.date.accessioned | 2023-10-24T19:24:02Z | |
dc.date.available | 2023-10-24T19:24:02Z | |
dc.date.created | 2023 | |
dc.identifier.issn | 13858947 | |
dc.identifier.uri | http://hdl.handle.net/11407/7911 | |
dc.description.abstract | Two engineered synthetic nanobody-based nanobiocomposite platforms were developed for label-free electrochemical detection of the epithelial growth factor receptor (EGFR) biomarker. Screen-printed carbon electrodes (SPCE) were decorated either with NiO nanoparticles (NPs) or poly(thiophene acetic acid) (PTAA) to link the anti-EGFR nanobody (Nb) and form nanobiocomposites for detecting the EGFR biomarker by electrochemical impedance spectroscopy (EIS). The nanoarchitectures were prepared by in situ electrosynthesis of NiO NPs or PTAA layers at SPCEs. A modified version of the 9G8 Nb (Nb9G8m), specific for the EGFR (anti-EGFR), was designed and produced as the nanobiosensor bioreceptor. This Nb was engineered to provide a hexahistidine tag (6xHis-tag) and a lysine (Lys) dual functionality to form a (6xHis-tag)/Ni2+ or Lys/PTAA interface. The biosensing interfaces were characterized by field-emission scanning electron microscopy, energy-dispersive X-ray spectroscopy, X-ray photoelectron spectroscopy, cyclic voltammetry, and EIS. The nanobody/nanobiocomposite-based biosensors detected EGFR proteins in a linear range from 0.25 to 50 μg mL−1 and 0.5 to 50 μg mL−1, with limits of detection of 0.46 μg mL−1 and 1.14 μg mL−1, for NiO- and PTAA-based platforms, respectively. The biosensing platforms offer high simplicity, specificity, and selectivity to detect EGFR, but Nbs can be readily engineered to detect other (glycol)proteins. Finally, as a proof of concept, the EGFR was detected in several tumor cell lines, differentiating biomarker expression among them. © 2023 Elsevier B.V. | eng |
dc.language.iso | eng | |
dc.publisher | Elsevier B.V. | |
dc.relation.isversionof | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85153612070&doi=10.1016%2fj.cej.2023.142941&partnerID=40&md5=f6363a1ab1f7ab62de5f0725ef35cd70 | |
dc.source | Chem. Eng. J. | |
dc.source | Chemical Engineering Journal | eng |
dc.subject | Biosensor | eng |
dc.subject | Electrochemical detection | eng |
dc.subject | Nanobody | eng |
dc.subject | Screen-printed electrode bioconjugation chemistry | eng |
dc.subject | XPS analysis | eng |
dc.title | Engineered synthetic nanobody-based biosensors for electrochemical detection of epidermal growth factor receptor | eng |
dc.type | Article | |
dc.rights.accessrights | info:eu-repo/semantics/restrictedAccess | |
dc.publisher.program | Ciencias Básicas | spa |
dc.type.spa | Artículo | |
dc.identifier.doi | 10.1016/j.cej.2023.142941 | |
dc.relation.citationvolume | 465 | |
dc.publisher.faculty | Facultad de Ciencias Básicas | spa |
dc.affiliation | Cruz-Pacheco, A.F., Max Planck Tandem Group in Nanobioengineering, Institute of Chemistry, Faculty of Natural and Exact Sciencies, University of Antioquia, Complejo Ruta N, Calle 67 No. 52-20, Medellín, 050010, Colombia | |
dc.affiliation | Monsalve, Y., Max Planck Tandem Group in Nanobioengineering, Institute of Chemistry, Faculty of Natural and Exact Sciencies, University of Antioquia, Complejo Ruta N, Calle 67 No. 52-20, Medellín, 050010, Colombia | |
dc.affiliation | Serrano-Rivero, Y., Faculty of Basic Sciences, University of Medellin, Medellin, 050026, Colombia | |
dc.affiliation | Salazar-Uribe, J., Faculty of Basic Sciences, University of Medellin, Medellin, 050026, Colombia | |
dc.affiliation | Moreno, E., Faculty of Basic Sciences, University of Medellin, Medellin, 050026, Colombia | |
dc.affiliation | Orozco, J., Max Planck Tandem Group in Nanobioengineering, Institute of Chemistry, Faculty of Natural and Exact Sciencies, University of Antioquia, Complejo Ruta N, Calle 67 No. 52-20, Medellín, 050010, Colombia | |
dc.relation.references | Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hammers, C., Songa, E.B., Bendahman, N., Hammers, R., Naturally occurring antibodies devoid of light chains (1993) Nature., 363, pp. 446-448 | |
dc.relation.references | Li, B., Qin, X., Mi, L.-Z., Nanobodies: from structure to applications in non-injectable and bispecific biotherapeutic development (2022) Nanoscale., 14, pp. 7110-7122 | |
dc.relation.references | Muyldermans, S., Nanobodies: Natural single-domain antibodies (2013) Annu. Rev. Biochem., 82, pp. 775-797 | |
dc.relation.references | Valdés-Tresanco, M.S., Molina-Zapata, A., Pose, A.G., Moreno, E., Structural Insights into the Design of Synthetic Nanobody Libraries (2022) Molecules., 27, pp. 1-18 | |
dc.relation.references | De Meyer, T., Muyldermans, S., Depicker, A., Nanobody-based products as research and diagnostic tools (2014) Trends Biotechnol., 32, pp. 263-270 | |
dc.relation.references | Zhou, Q., Li, G., Chen, K., Yang, H., Yang, M., Zhang, Y., Wan, Y., Zhang, Y., Simultaneous unlocking optoelectronic and interfacial properties of c60 for ultrasensitive immunosensing by coupling to metal-organic framework (2020) Anal. Chem., 92, pp. 983-990 | |
dc.relation.references | Pan, D., Li, G., Hu, H., Xue, H., Zhang, M., Zhu, M., Gong, X., Shen, Y., Direct Immunoassay for Facile and Sensitive Detection of Small Molecule Aflatoxin B1 based on Nanobody (2018) Chem. - A Eur. J., 24, pp. 9869-9876 | |
dc.relation.references | Zhou, Q., Li, G., Zhang, Y., Zhu, M., Wan, Y., Shen, Y., Highly Selective and Sensitive Electrochemical Immunoassay of Cry1C Using Nanobody and π-π Stacked Graphene Oxide/Thionine Assembly (2016) Anal. Chem., 88, pp. 9830-9836 | |
dc.relation.references | Kovalchuk, B., Berghoff, A.S., Karreman, M.A., Frey, K., Piechutta, M., Fischer, M., Grosch, J., Winkler, F., Nintedanib and a bi-specific anti-VEGF/Ang2 nanobody selectively prevent brain metastases of lung adenocarcinoma cells (2020) Clin. Exp. Metastasis., 37, pp. 637-648 | |
dc.relation.references | Liu, J., Jiang, Y., Chen, X., Chen, L., Zhang, X., Cui, D., Li, Y., Diao, A., Development of active affibody aggregates induced by a self-assembling peptide for high sensitive detection of alpha-fetoprotein (2022) Chem. Eng. J., 436 | |
dc.relation.references | Spinelli, S., Frenken, L.G.J., Hermans, P., Verrips, T., Brown, K., Tegoni, M., Cambillau, C., Aiguier, C.J., Camelid Heavy-Chain Variable Domains Provide Efficient Combining Sites to (2000) Biochemistry., 1217-1222 | |
dc.relation.references | Ganji, A., Islami, M., Ejtehadifar, M., Zarei-Mehrvarz, E., Darvish, M., Nanobody and aptamer as targeting moiety against bacterial toxins: Therapeutic and diagnostic applications (2019) Rev. Res. Med. Microbiol., 30, pp. 183-190 | |
dc.relation.references | An, N., Hou, Y.N., Zhang, Q.X., Li, T., Zhang, Q.L., Fang, C., Chen, H., Du, X., Anti-Multiple Myeloma Activity of Nanobody-Based Anti-CD38 Chimeric Antigen Receptor T Cells (2018) Mol. Pharm., 15, pp. 4577-4588 | |
dc.relation.references | Shu, M., Xu, Y., Wang, D., Liu, X., Li, Y., He, Q., Tu, Z., Wang, X., Anti-idiotypic nanobody: A strategy for development of sensitive and green immunoassay for Fumonisin B1 (2015) Talanta., 143, pp. 388-393 | |
dc.relation.references | Schumacher, D., Helma, J., Schneider, A.F.L., Leonhardt, H., Hackenberger, C.P.R., Nanobodies: Chemical Functionalization Strategies and Intracellular Applications (2018) Angew. Chemie - Int. Ed., 57, pp. 2314-2333 | |
dc.relation.references | Wang, L., Ding, Y., Li, N., Chai, Y., Li, Q., Du, Y., Hong, Z., Ou, L., Nanobody-based polyvinyl alcohol beads as antifouling adsorbents for selective removal of tumor necrosis factor-α (2022) Chinese Chem. Lett., 33, pp. 2512-2516 | |
dc.relation.references | Wu, W., Shi, L., Duan, Y., Xu, S., Shen, L., Zhu, T., Hou, L., Liu, B., Nanobody modified high-performance AIE photosensitizer nanoparticles for precise photodynamic oral cancer therapy of patient-derived tumor xenograft (2021) Biomaterials., 274 | |
dc.relation.references | Echeverri, D., Cruz-Pacheco, A.F., Orozco, J., Capacitive nanobiosensing of β-1,4- galactosyltransferase-V colorectal cancer biomarker (2023) Sensors Actuators: B. Chemical., 374, p. 132784 | |
dc.relation.references | Cajigas, S., Alzate, D., Orozco, J., Gold/DNA-based nanobioconjugate for electrochemical detection of zika virus (2020) Microchimica Acta, 187 (594) | |
dc.relation.references | Cruz‑Pacheco, A.F., Quinchia, J., Orozco, J., Nanostructured poly(thiophene acetic acid)/Au/poly(methylene blue) interface for electrochemical immunosensing of p53 protein (2023) Sensors Actuators: B. Chemical., 190, p. 136 | |
dc.relation.references | Cruz‑Pacheco, A.F., Quinchia, J., Orozco, J., Cerium oxide-doped PEDOT nanocomposite for label-free electrochemical immunosensing of anti-p53 autoantibodies (2022) Microchimica Acta, 189, p. 228 | |
dc.relation.references | Quinchia, J., Echeverri, D., Cruz-Pacheco, A.F., Maldonado, M.E., Orozco, J.A., Electrochemical biosensors for determination of colorectal tumor biomarkers (2020) Micromachines., 11, pp. 1-46 | |
dc.relation.references | Mashkoori, A., Mostafavi, A., Shamspur, T., Torkzadeh-Mahani, M., Electrochemical enzyme-based blood uric acid biosensor: new insight into the enzyme immobilization on the surface of electrode via poly-histidine tag (2022) Microchim. Acta., 189 | |
dc.relation.references | Meyerkord, C.L., Fu, H., (2015), Protein-protein interactions: Methods and applications: Second edition, Protein-Protein Interact. Methods Appl. Second Ed. 1278 1–613. doi: 10.1007/978-1-4939-2425-7 | |
dc.relation.references | Aydemir, N., Malmström, J., Travas-Sejdic, J., Conducting polymer based electrochemical biosensors (2016) Phys. Chem. Chem. Phys., 18, pp. 8264-8277 | |
dc.relation.references | Wee, P., Wang, Z., Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways (2017) Cancers (Basel), pp. 1-45 | |
dc.relation.references | Saif, M.W., Colorectal cancer in review: The role of the EGFR pathway (2010) Expert Opin. Investig. Drugs., 19, pp. 357-369 | |
dc.relation.references | Grant, S.L., Hammacher, A., Douglas, A.M., Goss, G.A., Mansfield, R.K., Heath, J.K., Begley, C.G., An unexpected biochemical and functional interaction between gp130 and the EGF receptor family in breast cancer cells (2002) Oncogene., 21, pp. 460-474 | |
dc.relation.references | Fischer, O.M., Hart, S., Gschwind, A., Ullrich, A., EGFR signal transactivation in cancer cells (2003) Biochem. Soc. Trans., 31, pp. 1203-1208 | |
dc.relation.references | Lin, G., Sun, X.J., Han, Q.B., Wang, Z., Xu, Y.P., Gu, J.L., Wu, W., Mao, W.M., Epidermal growth factor receptor protein overexpression and gene amplification are associated with aggressive biological behaviors of esophageal squamous cell carcinoma (2015) Oncol. Lett., 10, pp. 901-906 | |
dc.relation.references | McKay, J.A., Murray, L.J., Curran, S., Ross, V.G., Clark, C., Murray, G.I., Cassidy, J., McLeod, H.L., Evaluation of the epidermal growth factor receptor (EGFR) in colorectal tumours and lymph node metastases (2002) Eur. J. Cancer., 38, pp. 2258-2264 | |
dc.relation.references | Roovers, R.C., Vosjan, M.J.W.D., Laeremans, T., El Khoulati, R., De Bruin, R.C.G., Ferguson, K.M., Verkleij, A.J., P.m.p., Van Bergen En Henegouwen, A biparatopic anti-EGFR nanobody efficiently inhibits solid tumour growth (2011) Int. J. Cancer., 129, pp. 2013-2024 | |
dc.relation.references | Schmitz, K.R., Bagchi, A., Roovers, R.C., Van Bergen En, P.M.P., Henegouwen, K.M.F., Structural evaluation of EGFR inhibition mechanisms for nanobodies/VHH domains (2013) Structure., 21, pp. 1214-1224 | |
dc.relation.references | Noor, A., Walser, G., Wesseling, M., Giron, P., Laffra, A.-M., Haddouchi, F., De Grève, J., Kronenberger, P., Production of a mono-biotinylated EGFR nanobody in the E. coli periplasm using the pET22b vector (2018) BMC Res Notes, 11 (1) | |
dc.relation.references | Kaczmarek, J.Z., Skottrup, P.D., Selection and characterization of camelid nanobodies towards urokinase-type plasminogen activator (2015) Mol. Immunol., 65, pp. 384-390 | |
dc.relation.references | González Pose, A., Montesino Seguí, R., Maura Pérez, R., Hugues Salazar, F., Cabezas Ávila, I., Altamirano Gómez, C., Sánchez Ramos, O., Roberto Toledo, J., Characterisation of a new molecule based on two E2 sequences from bovine viral diarrhoea-mucosal disease virus fused to the human immunoglobulin Fc fragment (2021) J Vet. Res., 65, pp. 27-37 | |
dc.relation.references | Zach, M.P., Penner, R.M., Nanocrystalline nickel nanoparticles (2000) Adv. Mater., 12, pp. 878-883 | |
dc.relation.references | Huang, L.-F., Hutchison, M.J., Santucci, R.J., Scully, J.R., Rondinelli, J.M., Improved Electrochemical Phase Diagrams from Theory and Experiment: The Ni-Water System and Its Complex Compounds (2017) J. Phys. Chem. C., 121 (18), pp. 9782-9789 | |
dc.relation.references | Bartlett, P.N., Dawson, D.H., Electrochemistry of poly(3-thiopheneacetic acid) in aqueous solution: Evidence for an intramolecular chemical reaction (1994) J. Mater. Chem., 4, pp. 1805-1810 | |
dc.relation.references | Noorbakhsh, A., Salimi, A., Development of DNA electrochemical biosensor based on immobilization of ssDNA on the surface of nickel oxide nanoparticles modified glassy carbon electrode (2011) Biosens. Bioelectron., 30, pp. 188-196 | |
dc.relation.references | Ganesana, M., Istarnboulie, G., Marty, J.L., Noguer, T., Andreescu, S., Site-specific immobilization of a (His)6-tagged acetylcholinesterase on nickel nanoparticles for highly sensitive toxicity biosensors (2011) Biosens. Bioelectron., 30, pp. 43-48 | |
dc.relation.references | Kaszuba, K., Grzybek, M., Orłowski, A., Danne, R., Róg, T., Simons, K., Coskun, Ü., Vattulainen, I., N-Glycosylation as determinant of epidermal growth factor receptor conformation in membranes (2015) Proc. Natl. Acad. Sci. U. S. A., 112, pp. 4334-4339 | |
dc.relation.references | Brett, C.M.A., Electrochemical Impedance Spectroscopy in the Electrochemical Sensors and Biosensors (2022) Molecules., 27, p. 1497 | |
dc.relation.references | Weidler, N., Schuch, J., Knaus, F., Stenner, P., Hoch, S., Maljusch, A., Schäfer, R., Jaegermann, W., X-ray Photoelectron Spectroscopic Investigation of Plasma-Enhanced Chemical Vapor Deposited NiOx, NiOx(OH)y, and CoNiOx(OH)y: Influence of the Chemical Composition on the Catalytic Activity for the Oxygen Evolution Reaction (2017) J. Phys. Chem. C., 121, pp. 6455-6463 | |
dc.relation.references | Eby, D.M., Artyushkova, K., Paravastu, A.K., Johnson, G.R., Probing the molecular structure of antimicrobial peptide-mediated silica condensation using X-ray photoelectron spectroscopy (2012) J. Mater. Chem., 22, pp. 9875-9883 | |
dc.relation.references | Wasserberg, D., Cabanas-Danés, J., Prangsma, J., O'Mahony, S., Cazade, P.A., Tromp, E., Blum, C., Jonkheijm, P., Controlling Protein Surface Orientation by Strategic Placement of Oligo-Histidine Tags (2017) ACS Nano., 11, pp. 9068-9083 | |
dc.relation.references | Qiu, X., Wegner, K.D., Wu, Y.T., Van Bergen En, P.M.P., Henegouwen, T.L., Jennings, N.H., Nanobodies and antibodies for duplexed EGFR/HER2 immunoassays using terbium-to-quantum dot FRET (2016) Chem. Mater., 28, pp. 8256-8267 | |
dc.relation.references | Wegner, K.D., Lindén, S., Jin, Z., Jennings, T.L., El Khoulati, R., Van Bergen En, P.M.P., Henegouwen, N.H., Nanobodies and nanocrystals: Highly sensitive quantum dot-based homogeneous FRET immunoassay for serum-based EGFR detection (2014) Small., 10, pp. 734-740 | |
dc.relation.references | Schmidt-Ullrich, R.K., Mikkelsen, R.B., Dent, P., Todd, D.G., Valerie, K., Kavanagh, B.D., Contessa, J.N., Chen, P.B., Radiation-induced proliferation of the human A431 squamous carcinoma cells is dependent on EGFR tyrosine phosphorylation (1997) Oncogene., 15, pp. 1191-1197 | |
dc.relation.references | Wang, Z., Zhang, X., Yang, Z., Du, H., Wu, Z., Gong, J., Yan, J., Zheng, Q., MiR-145 regulates PAK4 via the MAPK pathway and exhibits an antitumor effect in human colon cells (2012) Biochem. Biophys. Res. Commun., 427, pp. 444-449 | |
dc.relation.references | Xu, Y., Soo, P., Walker, F., Zhang, H.H., Redpath, N., Tan, C.W., Nicola, N.A., Burgess, A.W., LRIG1 extracellular domain: Structure and function analysis (2015) J. Mol. Biol., 427, pp. 1934-1948 | |
dc.relation.references | Li, Y., Sun, Z., Liu, B., Shan, Y., Zhao, L., Jia, L.I., Tumor-suppressive miR-26A and miR-26B inhibit cell aggressiveness by regulating fut4 in colorectal cancer (2017) Cell Death Dis., 8 (6), pp. e2892-e | |
dc.relation.references | Holbro, T., Beerli, R.R., Maurer, F., Koziczak, M., Barbas, C.F., Hynes, N.E., The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation (2003) Proc. Natl. Acad. Sci. U.S.A., 100 (15), pp. 8933-8938 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | |
dc.identifier.reponame | reponame:Repositorio Institucional Universidad de Medellín | |
dc.identifier.repourl | repourl:https://repository.udem.edu.co/ | |
dc.identifier.instname | instname:Universidad de Medellín |
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