Evidence map›Paper›PMID 36593927›Full record

ArticleCurrent research in pharmacology and drug discovery2023

A new triphenylphosphonium-conjugated amphipathic cationic peptide with improved cell-penetrating and ROS-targeting properties.

Rezeda A Ishkaeva, Diana V Salakhieva, Ruslan Garifullin, Raghad Alshadidi, Alexander V Laikov, Abdulla A Yergeshov, Marat I Kamalov, Timur I Abdullin

Open access · goldAbstract read
In one paragraph

Article in Current research in pharmacology and drug discovery, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
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  5. Biological Activities ofInternational journal of molecular sciences · 2023
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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

8 authors at 1 institution in 2 countries.

Rezeda A IshkaevaDepartment of Biochemistry, Biotechnology, Pharmacology, Institute of Fundamental Medicine and Biology, Kazan Volga Region Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russia.
Diana V SalakhievaDepartment of Biochemistry, Biotechnology, Pharmacology, Institute of Fundamental Medicine and Biology, Kazan Volga Region Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russia.
Ruslan GarifullinDepartment of Biochemistry, Biotechnology, Pharmacology, Institute of Fundamental Medicine and Biology, Kazan Volga Region Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russia.
Raghad AlshadidiDepartment of Biochemistry, Biotechnology, Pharmacology, Institute of Fundamental Medicine and Biology, Kazan Volga Region Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russia.
Alexander V LaikovDepartment of Biochemistry, Biotechnology, Pharmacology, Institute of Fundamental Medicine and Biology, Kazan Volga Region Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russia.
Abdulla A YergeshovDepartment of Biochemistry, Biotechnology, Pharmacology, Institute of Fundamental Medicine and Biology, Kazan Volga Region Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russia.
Marat I KamalovDepartment of Biochemistry, Biotechnology, Pharmacology, Institute of Fundamental Medicine and Biology, Kazan Volga Region Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russia.
Timur I AbdullinDepartment of Biochemistry, Biotechnology, Pharmacology, Institute of Fundamental Medicine and Biology, Kazan Volga Region Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russia.
Kazan Federal University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We study for the first time whether triphenylphosphonium (TPP) moiety can improve cellular delivery and redox properties of amphipathic cationic peptides based on YRFK/YrFK cell-penetrating and cytoprotective motif. TPP moiety was found to increase reducing activity of both stereoisomeric peptides in solution and on electrode surface in association with TPP-mediated intramolecular interactions. Among TPP-conjugated peptides, newly synthesized TPP3-YrFK featured both increased antioxidant efficacy and proteolytic resistance. TPP-conjugated peptides preferably mitigated endogenic ROS in mitochondria and cytoplasm of model glioblastoma cells with increased oxidative status. This anti-ROS effect was accompanied by mild reversible decrease of reduced glutathione level in the cells with relatively weak change in glutathione redox forms ratio. Such low interference with cell redox status is in accordance with non-cytotoxic nature of the compounds. Intracellular concentrations of label-free peptides were analyzed by LC-MS/MS, which showed substantial TPP-promoted penetration of YrFK motif across cell plasma membrane. However, according to ΔΨ

Indexed as

aa, amino acidABTS, 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)Amphipathic cationic peptidesCCCP, carbonyl cyanide 3-chlorophenylhydrazoneCD, circular dichroismCellular pharmacokineticsDCFDA, 2′,7′-dichlorofluorescin diacetateGSH, reduced glutathioneHBSS, Hank's balanced salt solutionIntramolecular interactionLC–MS/MS, liquid chromatography tandem mass-spectrometryMCB, monochlorobimaneMRM, multiple reaction monitoringRedox activityROS, reactive oxygen speciesROS targetingSPPS, solid-phase peptide synthesisTPP, triphenylphosphoniumTriphenylphosphonium cation

Identifiers

PMID36593927
PMCPMC9804109
OpenAlexW4312056156

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.