Evidence map›Paper›PMID 33782419›Full record

ArticleScientific reports2021

Non-covalently embedded oxytocin in alkanethiol monolayer as Zn

Jessica Attia, Sivan Nir, Evgeniy Mervinetsky, Dora Balogh, Agata Gitlin-Domagalska, Israel Alshanski, Meital Reches, Mattan Hurevich, Shlomo Yitzchaik

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2021. 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
0.4field-weighted citation impact, top 41% of its field
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, 5 citations in OpenAlex.

  1. Article
  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

9 authors at 2 institutions in 2 countries.

Jessica Attia *The Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, 91904, Jerusalem, Israel.
Sivan Nir *The Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, 91904, Jerusalem, Israel.
Evgeniy Mervinetsky *The Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, 91904, Jerusalem, Israel.
Dora BaloghThe Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, 91904, Jerusalem, Israel.
Agata Gitlin-DomagalskaThe Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, 91904, Jerusalem, Israel.
Israel AlshanskiThe Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, 91904, Jerusalem, Israel.
Meital RechesThe Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, 91904, Jerusalem, Israel. Meital.reches@mail.huji.ac.il.
Mattan HurevichThe Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, 91904, Jerusalem, Israel. Mattan.hurevich@mail.huji.ac.il.
Shlomo YitzchaikThe Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, 91904, Jerusalem, Israel. Shlomo.Yitzchaik@mail.huji.ac.il.
Hebrew University of Jerusalem · ILUniversity of Gdańsk · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptides are commonly used as biosensors for analytes such as metal ions as they have natural binding preferences. In our previous peptide-based impedimetric metal ion biosensors, a monolayer of the peptide was anchored covalently to the electrode. Binding of metal ions resulted in a conformational change of the oxytocin peptide in the monolayer, which was measured using electrochemical impedance spectroscopy. Here, we demonstrate that sensing can be achieved also when the oxytocin is non-covalently integrated into an alkanethiol host monolayer. We show that ion-binding cause morphological changes to the dense host layer, which translates into enhanced impedimetric signals compared to direct covalent assembly strategies. This biosensor proved selective and sensitive for Zn

Indexed as

Biosensing TechniquesDielectric SpectroscopyHydrophobic and Hydrophilic InteractionsLimit of DetectionMicroscopy, Atomic ForceOxytocinSulfhydryl CompoundsZincOxytocinSulfhydryl CompoundsZinc

Identifiers

PMID33782419
PMCPMC8007701
OpenAlexW3146467598

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.