Evidence map›Paper›PMID 39542433›Full record

ArticleAnalytical chemistry2024

Synthetic Protein-to-DNA Input Exchange for Protease Activity Detection Using CRISPR-Cas12a.

Luca Capelli, Federica Pedrini, Andrea C Di Pede, Alejandro Chamorro-Garcia, Neda Bagheri, Simone Fortunati, Marco Giannetto, Monica Mattarozzi, Roberto Corradini, Alessandro Porchetta and 1 more

Abstract read
In one paragraph

Article in Analytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. MARPLE: A Proximity-Triggered CRISPR-Cas13 Platform for Ultrasensitive Antibody Detection.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Article
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

11 authors.

Luca CapelliDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parco Area Delle Scienze 17/A, 43124 Parma, Italy.
Federica PedriniDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parco Area Delle Scienze 17/A, 43124 Parma, Italy.
Andrea C Di PedeDepartment of Chemistry, University of Rome Tor Vergata, Via della Ricerca Scientifica 1, 00133 Rome, Italy.
Alejandro Chamorro-GarciaDepartment of Chemistry, University of Rome Tor Vergata, Via della Ricerca Scientifica 1, 00133 Rome, Italy.
Neda BagheriDepartment of Chemistry, University of Rome Tor Vergata, Via della Ricerca Scientifica 1, 00133 Rome, Italy.ORCID 0009-0005-0805-8201
Simone FortunatiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parco Area Delle Scienze 17/A, 43124 Parma, Italy.
Marco GiannettoDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parco Area Delle Scienze 17/A, 43124 Parma, Italy.ORCID 0000-0001-7031-7466
Monica MattarozziDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parco Area Delle Scienze 17/A, 43124 Parma, Italy.ORCID 0000-0002-6766-4616
Roberto CorradiniDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parco Area Delle Scienze 17/A, 43124 Parma, Italy.ORCID 0000-0002-8026-0923
Alessandro PorchettaDepartment of Chemistry, University of Rome Tor Vergata, Via della Ricerca Scientifica 1, 00133 Rome, Italy.ORCID 0000-0002-4061-5574
Alessandro BertucciDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parco Area Delle Scienze 17/A, 43124 Parma, Italy.ORCID 0000-0003-4842-9909

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present a novel activity-based detection strategy for matrix metalloproteinase 2 (MMP2), a critical cancer protease biomarker, leveraging a mechanism responsive to the proteolytic activity of MMP2 and its integration with CRISPR-Cas12a-assisted signal amplification. We designed a chemical translator comprising two functional units─a peptide and a peptide nucleic acid (PNA), fused together. The peptide presents the substrate of MMP2, while the PNA serves as a nucleic acid output for subsequent processing. This chemical translator was immobilized on micrometer magnetic beads as a physical support for an activity-based assay. We incorporated into our design a single-stranded DNA partially hybridized with the PNA sequence and bearing a region complementary to the RNA guide of CRISPR-Cas12a. The target-induced nuclease activity of Cas12a results in the degradation of FRET-labeled DNA reporters and amplified fluorescence signal, enabling the detection of MMP2 in the low picomolar range, showing a limit of detection of 72 pg/mL. This study provides new design principles for a broader applicability of CRISPR-Cas-based biosensing.

Indexed as

CRISPR-Cas SystemsMatrix Metalloproteinase 2Biosensing TechniquesCRISPR-Associated ProteinsDNADNA, Single-StrandedFluorescence Resonance Energy TransferHumansPeptide Nucleic AcidsPeptidesCRISPR-Associated ProteinsDNADNA, Single-StrandedMatrix Metalloproteinase 2MMP2 protein, humanPeptide Nucleic AcidsPeptides

Identifiers

PMID39542433
PMCPMC11603406

What OpenQuestion holds

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Registered trials

None linked

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.