Evidence map›Paper›PMID 38713296›Full record

ArticleMikrochimica acta2024

Turn-off enzyme activity of histidine-rich peptides for the detection of lysozyme.

Zu-Han Yang, Ling-Fang Huang, Yi-Shan Wang, Chia-Chen Chang

Abstract read
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In one paragraph

Article in Mikrochimica acta, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

4 authors.

Zu-Han YangDepartment of Medical Biotechnology and Laboratory Science, Chang Gung University, Taoyuan, 333, Taiwan.
Ling-Fang HuangDepartment of Medical Biotechnology and Laboratory Science, Chang Gung University, Taoyuan, 333, Taiwan.
Yi-Shan WangDepartment of Medical Biotechnology and Laboratory Science, Chang Gung University, Taoyuan, 333, Taiwan.
Chia-Chen ChangDepartment of Medical Biotechnology and Laboratory Science, Chang Gung University, Taoyuan, 333, Taiwan. chang@cgu.edu.tw.ORCID http://orcid.org/0000-0001-5466-4724

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An assay that integrates histidine-rich peptides (HisRPs) with high-affinity aptamers was developed enabling the specific and sensitive determination of the target lysozyme. The enzyme-like activity of HisRP is inhibited by its interaction with a target recognized by an aptamer. In the presence of the target, lysozyme molecules progressively assemble on the surface of HisRP in a concentration-dependent manner, resulting in the gradual suppression of enzyme-like activity. This inhibition of HisRP's enzyme-like activity can be visually observed through color changes in the reaction product or quantified using UV-visible absorption spectroscopy. Under optimal conditions, the proposed colorimetric assay for lysozyme had a detection limit as low as 1 nM and exhibited excellent selectivity against other nonspecific interferents. Furthermore, subsequent research validated the practical applicability of the developed colorimetric approach to saliva samples, indicating that the assay holds significant potential for the detection of lysozymes in samples derived from humans.

Indexed as

ColorimetryMuramidaseSalivaAptamers, NucleotideBiosensing TechniquesHistidineHistidine-Rich GlycoproteinHumansLimit of DetectionPeptidesProteinsAptamers, NucleotideHistidineHistidine-Rich GlycoproteinMuramidasePeptidesProteinsColorimetric assayHistidine-rich peptideLysozyme aptamerLysozyme determination

Identifiers

PMID38713296

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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.