Evidence map›Paper›PMID 41228903›Full record

ArticleSensors (Basel, Switzerland)2025

Engineering Linker-Enhanced OmpG Nanopores for Rapid Single-Molecule Protease Detection.

Minji Kim, Bach Pham

Abstract read
In one paragraph

Article in Sensors (Basel, Switzerland), 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

2 authors.

Minji KimFood Science Department, University of Massachusetts Amherst, Amherst, MA 01003, USA.ORCID 0000-0002-8926-9449
Bach PhamDepartment of Chemistry, University of Science, Vietnam National University, Hanoi 11000, Vietnam.

Funding

National Research Foundation of Korea RS-2021-NR060118
6 · The paper itself

Abstract

Single-molecule nanopore sensors have enabled real-time detection of enzymatic cleavage events, yet achieving sensitive and specific analysis of protease activity remains an important challenge for diagnostic applications. We engineered OmpG nanopore constructs incorporating thrombin recognition peptides into loop 6 with varied flexible and negatively charged linkers to optimize accessibility and cleavage. SDS-PAGE gel analysis showed that constructs with the recognition peptide placed after residue D225 and incorporating dual linkers achieved cleavage efficiencies up to 95%, whereas constructs without linkers showed limited cleavage. Single-channel recordings revealed that linker integration modulates pore conductance, with extended loops exhibiting intermediate open-state currents near 18 pA compared to 25 pA in wild-type OmpG. Upon thrombin addition, rapid and irreversible current drops confirmed real-time protease activity detection. These results demonstrate the critical role of linker design, particularly flexibility and charge, in optimizing nanopore protease sensors, providing a versatile platform for biomedical applications.

Indexed as

Bacterial Outer Membrane ProteinsBiosensing TechniquesEscherichia coli ProteinsNanoporesPeptide HydrolasesThrombinBacterial Outer Membrane ProteinsEscherichia coli ProteinsPeptide HydrolasesThrombincleavage efficacynanopore sensorouter membrane protein G (OmpG)peptide linkersingle-channel recordingsingle-molecular sensing

Identifiers

PMID41228903
PMCPMC12610258

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.