Evidence map›Paper›PMID 40859802›Full record

ArticleAnalytical chemistry2025

Functional Raman Probes for Detecting Enzyme Activities Based on Aggregation Control.

Momoko Okinaka, Minoru Kawatani, Hiroyoshi Fujioka, Spencer John Spratt, Hiroki Ito, Yoshihiro Misawa, Reika Otake, Aoi Ishikawa, Ryosuke Kojima, Yasuteru Urano and 2 more

Abstract read
In one paragraph

Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
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.

Momoko OkinakaGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
Minoru KawataniLaboratory for Chemistry and Life Science, Institute of Integrated Research, Institute of Science Tokyo, Yokohama, Kanagawa 226-8501, Japan.ORCID 0000-0002-0192-4366
Hiroyoshi FujiokaLaboratory for Chemistry and Life Science, Institute of Integrated Research, Institute of Science Tokyo, Yokohama, Kanagawa 226-8501, Japan.ORCID 0000-0003-1904-0566
Spencer John SprattResearch Center for Advanced Science and Technology, The University of Tokyo, Tokyo 153-8904, Japan.
Hiroki ItoGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
Yoshihiro MisawaGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
Reika OtakeLaboratory for Chemistry and Life Science, Institute of Integrated Research, Institute of Science Tokyo, Yokohama, Kanagawa 226-8501, Japan.
Aoi IshikawaDepartment of Life Science and Technology, Institute of Science Tokyo, Yokohama, Kanagawa 226-8501, Japan.
Ryosuke KojimaGraduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.ORCID 0000-0002-3792-9222
Yasuteru UranoGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.ORCID 0000-0002-1220-6327
Yasuyuki OzekiResearch Center for Advanced Science and Technology, The University of Tokyo, Tokyo 153-8904, Japan.ORCID 0000-0002-9004-0799
Mako KamiyaLaboratory for Chemistry and Life Science, Institute of Integrated Research, Institute of Science Tokyo, Yokohama, Kanagawa 226-8501, Japan.ORCID 0000-0002-5592-1849

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Visualizing specific enzyme activities in living systems is important in biomedical research, and Raman imaging probes are particularly suitable for simultaneous multiplexed detection of plural enzyme activities due to their narrow signal peak widths. Here, we present a molecular design strategy for enzyme-activity-detecting Raman probes based on control of aggregation. The probe itself is soluble and diffusive in aqueous solution due to its hydrophilic substrate moiety, but hydrolysis by the target enzyme affords a hydrophobic product that forms aggregates, thereby increasing the local dye concentration, which in turn results in a stronger Raman signal that enables visualization of the enzyme activity. We validated the molecular design by developing Raman probes targeting aminopeptidase, glycosidase and carboxypeptidase. The vibrational frequency can be shifted by isotope-editing, and the developed probes were successfully applied to visualize the activities of aminopeptidase and glycosidase in live cultured cells and spheroids.

Indexed as

AminopeptidasesGlycoside HydrolasesMolecular ProbesSpectrum Analysis, RamanAnimalsHumansAminopeptidasesGlycoside HydrolasesMolecular Probes

Identifiers

PMID40859802
PMCPMC12424018

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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.