Evidence map›Paper›PMID 37514647›Full record

ArticleSensors (Basel, Switzerland)2023

In Situ Monitoring of Aptamer-Protein Binding on a ZnO Surface Using Spectroscopic Ellipsometry.

Adeem Alshammari, Harm van Zalinge, Ian Sandall

Abstract read
In one paragraph

Article in Sensors (Basel, Switzerland), 2023. 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

3 authors.

Adeem AlshammariDepartment of Electrical Engineering & Electronics, University of Liverpool, Liverpool L69 3GJ, UK.ORCID 0009-0001-9415-3088
Harm van ZalingeDepartment of Electrical Engineering & Electronics, University of Liverpool, Liverpool L69 3GJ, UK.ORCID 0000-0003-0996-1281
Ian SandallDepartment of Electrical Engineering & Electronics, University of Liverpool, Liverpool L69 3GJ, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dissolution of zinc oxide is investigated using spectroscopic ellipsometry to investigate its suitability as a platform for biosensing applications. The results indicate that once the ZnO surface has been functionalised, it is suitably protected, and no significant dissolving of the ZnO occurs. The binding kinetics of the SARS-CoV-2 spike protein on aptamer-functionalised zinc oxide surfaces are subsequently investigated. Values are extracted for the refractive index and associated optical constants for both the aptamer layer used and the protein itself. It is shown that upon an initial exposure to the protein, a rapid fluctuation in the surface density is observed. After around 20 min, this effect stabilises, and a fixed increase in the surface density is observed, which itself increases as the concentration of the protein is increased. This technique and setup are demonstrated to have a limit-of-detection down to 1 nanomole (nM) and display a linear response to concentrations up to 100 nM.

Indexed as

Aptamers, NucleotideBiosensing TechniquesCOVID-19Zinc OxideHumansProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusAptamers, NucleotideSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Zinc Oxideaptamersbiosensorsellipsometry

Identifiers

PMID37514647
PMCPMC10385375

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.