ArticleRSC advances2018
Effects of proton conduction on dielectric properties of peptides.
Article in RSC advances, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
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.
Who cites it
1 citing paper in PubMed, 13 citations in OpenAlex.
- Synaptic transistors based on a tyrosine-rich peptide for neuromorphic computing.RSC advances · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptides have been overlooked for their use in the field of electronics, even though they are one of the most commonly found bio-induced materials, and are not only easy to mass-produce but also exhibit a high dielectric constant. Additionally, unlike proteins, which are gaining considerable interest with materials researchers, peptides are much simpler, rendering their original characteristics easier to maintain without significant alteration of their structure. On the other hand, proteins tend to deform due to their susceptibility to environmental changes. Combining such superb dielectric properties with their relatively stable nature, peptides could be utilized as a component of electronic devices ranging from basic capacitors to more complex thin-film transistors. In this paper, a peptide chain (YYACAYY) composed of tyrosine, alanine, and cysteine was extensively studied using an impedance analyzer to determine its innate charge movement mechanism in order to extend our understanding of the electric properties of peptides. The movement of mobile protons inside the peptide insulator was found to be the source of the high relative permittivity of the peptide insulator, and the dielectric constant of the peptide insulator was found to be over 17 in humid conditions. By widening the understanding of the dielectric properties of the peptide insulator, it is expected that the peptide can be further utilized as an insulator in various electronic devices.
Identifiers
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Registered trials
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.