journal article·2026Open access

Film, function, flexibility: label-free nanobody sensors via electropolymerized nanointerfaces

Daniel P. Carroll, Imen Boumar, Anna M. Kotowska, David J. Scurr, Paula M. Mendes

Nanoscale· Volume 18· Issue 19

Abstract

Nanobody-based biosensors promise exceptional molecular recognition and robustness, but their implementation has been limited by unstable and non-scalable surface chemistries. Here we introduce a materials platform that integrates stable electropolymerized tyramine nanofilms with label-free, non-faradaic electrochemical impedance spectroscopy for direct molecular detection. The electropolymerized nanofilms form amine-functionalized coatings that are electrically insulating yet chemically active, supporting site-specific covalent immobilization of nanobodies in controlled orientations. Target binding induces more than a 50% increase in the capacitance signal response, providing a distinct label-free signature of molecular recognition. The platform can be adapted to diverse bioreceptors and antifouling layers, offering a general route to chemically robust and scalable bioelectronic interfaces. By decoupling film conductivity from functional stability, this work establishes a new class of interfaces that bridge molecular design with label-free signal transduction for next-generation biosensing technologies.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Polymer Surface Interaction Studies · Conducting polymers and applications · Polydiacetylene-based materials and applications

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

School of Chemical Engineering, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK

School of Pharmacy, University of Nottingham, Nottingham, NG7 2RD, UK

Funding

Engineering and Physical Sciences Research Council · UK Research and Innovation · H2020 European Research Council

References (32)

Show source-provided references
1. Campuzano · Anal. Sens. · 2023 · 3 · e202200087
2. Gavrilas · Sensors · 2022 · 22 · 151310.3390/s22041513 ↗
3. Curulli · Molecules · 2021 · 26 · 294010.3390/molecules26102940 ↗
4. Yu · Biomater. Sci. · 2020 · 8 · 355910.1039/D0BM00574F ↗
5. Tillib · Mol. Biol. · 2020 · 54 · 31710.1134/S0026893320030164 ↗
6. Chen · Talanta · 2016 · 147 · 52310.1016/j.talanta.2015.10.027 ↗
7. Gonzalez-Sapienza · Front. Immunol. · 2017 · 8 · 97710.3389/fimmu.2017.00977 ↗
8. S.Muyldermans , Nanobodies: Natural Single-Domain Antibodies , in Annual Review of Biochemistry , ed. R. D. Kornberg , Annual Review of Biochemistry , 2013 , vol. 82 , pp. 775–797
9. Guo · Nat. Biomed. Eng. · 2021 · 5 · 66610.1038/s41551-021-00734-9 ↗
10. Koklu · Adv. Mater. · 2022 · 34 · 220297210.1002/adma.202202972 ↗
11. Zhang · ACS Nano · 2023 · 17 · 916710.1021/acsnano.2c12733 ↗
12. Talwar · Chem. Eng. J. · 2025 · 525 · 17001710.1016/j.cej.2025.170017 ↗
13. Hu · Anal. Chem. · 2024 · 96 · 1967810.1021/acs.analchem.4c04826 ↗
14. Li · Sci. Total Environ. · 2021 · 753 · 14195010.1016/j.scitotenv.2020.141950 ↗
15. Yi · Sci. Rep. · 2025 · 15 · 78510.1038/s41598-024-83869-4 ↗
16. Simões · ACS Appl. Mater. Interfaces · 2021 · 13 · 1735310.1021/acsami.1c02280 ↗
17. Carroll · Curr. Opin. Electrochem. · 2023 · 40 · 10131910.1016/j.coelec.2023.101319 ↗
18. Sun · Nano Lett. · 2006 · 6 · 34510.1021/nl052130h ↗
19. Lee · Langmuir · 1998 · 14 · 641910.1021/la980724c ↗
20. Su · MedComm: Biomater. Appl. · 2023 · 2 · e54
21. Lisdat · Anal. Bioanal. Chem. · 2008 · 391 · 155510.1007/s00216-008-1970-7 ↗
22. Stevenson · SLAS Technol. · 2018 · 23 · 510.1177/2472630317738700 ↗
23. Zhao · Phys. Rev. B: Condens. Matter Mater. Phys. · 1999 · 60 · 915710.1103/PhysRevB.60.9157 ↗
24. Kirchhain · Trends Anal. Chem. · 2020 · 133 · 11607310.1016/j.trac.2020.116073 ↗
25. Lakard · Appl. Sci. · 2020 · 10 · 661410.3390/app10186614 ↗
26. Hicks · Langmuir · 2017 · 33 · 492410.1021/acs.langmuir.7b00494 ↗
27. Luong · J. Funct. Biomater. · 2020 · 11 · 7110.3390/jfb11040071 ↗
28. G. T.Hermanson , Bioconjugate Techniques , Academic Press , Boston , 3rd edn, 2013
29. Di Palma · ACS Appl. Mater. Interfaces · 2019 · 11 · 893710.1021/acsami.9b00927 ↗
30. Simões · ACS Appl. Mater. Interfaces · 2021 · 13 · 1735310.1021/acsami.1c02280 ↗
31. Berman · Surf. Interface Anal. · 2009 · 41 · 9710.1002/sia.2953 ↗
32. Kubala · Protein Sci. · 2010 · 19 · 238910.1002/pro.519 ↗