Evidence map›Paper›PMID 41149322›Full record

ArticleBiosensors2025

Affinity-Based Copolymer Coating for Oriented Protein Immobilization in Biosensor Development.

Lorenzo Zarini, Thomas Carzaniga, Morena Pirotta, Francesco Damin, Dario Brambilla, Marcella Chiari, Ivan Bassanini, Paola Gagni, Alessandro Mussida, Luca Casiraghi and 2 more

Abstract read
In one paragraph

Article in Biosensors, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Lorenzo ZariniInstitute of Chemical and Technological Sciences "Giulio Natta", National Research Council of Italy, Via Mario Bianco 9, 20131 Milan, Italy.ORCID 0009-0008-0082-2289
Thomas CarzanigaDepartment of Medical Biotechnology and Translational Medicine, Università degli Studi di Milano, 20054 Segrate, Italy.ORCID 0000-0002-4236-4019
Morena PirottaInstitute of Chemical and Technological Sciences "Giulio Natta", National Research Council of Italy, Via Mario Bianco 9, 20131 Milan, Italy.
Francesco DaminInstitute of Chemical and Technological Sciences "Giulio Natta", National Research Council of Italy, Via Mario Bianco 9, 20131 Milan, Italy.ORCID 0000-0003-1780-7823
Dario BrambillaInstitute of Chemical and Technological Sciences "Giulio Natta", National Research Council of Italy, Via Mario Bianco 9, 20131 Milan, Italy.ORCID 0000-0003-3490-4481
Marcella ChiariInstitute of Chemical and Technological Sciences "Giulio Natta", National Research Council of Italy, Via Mario Bianco 9, 20131 Milan, Italy.ORCID 0000-0002-4670-1430
Ivan BassaniniInstitute of Chemical and Technological Sciences "Giulio Natta", National Research Council of Italy, Via Mario Bianco 9, 20131 Milan, Italy.ORCID 0000-0001-9589-3689
Paola GagniInstitute of Chemical and Technological Sciences "Giulio Natta", National Research Council of Italy, Via Mario Bianco 9, 20131 Milan, Italy.ORCID 0000-0002-3652-6173
Alessandro MussidaInstitute of Chemical and Technological Sciences "Giulio Natta", National Research Council of Italy, Via Mario Bianco 9, 20131 Milan, Italy.
Luca CasiraghiDepartment of Medical Biotechnology and Translational Medicine, Università degli Studi di Milano, 20054 Segrate, Italy.
Marco BuscagliaDepartment of Medical Biotechnology and Translational Medicine, Università degli Studi di Milano, 20054 Segrate, Italy.ORCID 0000-0001-5010-0278
Laura SolaInstitute of Chemical and Technological Sciences "Giulio Natta", National Research Council of Italy, Via Mario Bianco 9, 20131 Milan, Italy.ORCID 0000-0002-2603-0318

Funding

EU Horizon Europe Research and Innovation Programme 101095426Ministero dell'Università e della Ricerca 2022EJL28BMinistero dell'Università e della Ricerca 2022H7MH23Ministero dell'Università e della Ricerca 2022YYLSJ2Ministero dell'Università e della Ricerca CN00000041
6 · The paper itself

Abstract

Effective protein immobilization is a critical step in biosensor development, as it ensures the stability, functionality, and orientation of biomolecules on the sensor surface. Here, we present a novel affinity-based terpolymer coating designed to enhance protein immobilization for biosensor applications. The novelty lies in the incorporation of nitrilotriacetic acid (NTA) ligands directly into the polymeric chains, facilitating histidine-tagged protein oriented binding through a robust metal-chelating interaction. To validate the system, magnetic microbeads coated with the polymer were tested for their ability to bind native and His-tagged proteins. The results demonstrated the superior binding capacity, enhanced stability, and reversibility of the interactions compared to traditional coatings, which immobilize proteins through nucleophile reactions with amine residues. Moreover, enzyme immobilization tests confirmed that the polymer preserves enzymatic activity, highlighting its potential for biosensor applications requiring functional biomolecules. This innovative polymeric coating offers a fast, versatile, and scalable solution for next-generation biosensor platforms, paving the way for improved sensitivity, reliability, and accessibility in diagnostic and analytical technologies.

Indexed as

Biosensing TechniquesImmobilized ProteinsPolymersEnzymes, ImmobilizedNitrilotriacetic AcidEnzymes, ImmobilizedImmobilized ProteinsNitrilotriacetic AcidPolymersbiosensorhis-tag proteinmicroarrayNTAprotein immobilizationsurface coating

Identifiers

PMID41149322
PMCPMC12564766

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.