Thermochemical Study of the Interaction of Cytosine and Uracil with Peptides in a Buffered Saline: Complex Formation with beta-Endorphin 30-31 (Human), L-Glutathion (Reduced) and α-L-Alanyl-L-Tyrosine.

Vladimir P Barannikov, Valeriy I Smirnov, Igor N Mezhevoi, Damir R Koltyshev

Abstract read

In one paragraph

Article in International journal of molecular sciences, 2023. 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.

DFT-calculations and RDG analysis (topology) of complexes between glutathione and nucleic bases of pyrymidine series.Journal of molecular modeling · 2025
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.

Vladimir P BarannikovG.A. Krestov Institute of Solution Chemistry, Russian Academy of Science, 153045 Ivanovo, Russia.ORCID 0000-0002-5778-4120

Valeriy I SmirnovG.A. Krestov Institute of Solution Chemistry, Russian Academy of Science, 153045 Ivanovo, Russia.

Igor N MezhevoiG.A. Krestov Institute of Solution Chemistry, Russian Academy of Science, 153045 Ivanovo, Russia.ORCID 0000-0002-0215-3444

Damir R KoltyshevG.A. Krestov Institute of Solution Chemistry, Russian Academy of Science, 153045 Ivanovo, Russia.

Funding

Russian Science Foundation 22-23-01118

6 · The paper itself

Abstract

The complex formation of uracil and cytosine with glycyl-L-glutamic acid (β-endorphin 30-31), γ-L-glutamyl-L-cysteinyl-glycine (glutathione reduced), α-L-alanyl-L-tyrosine, and α-L-alanyl-α-L-alanine in a buffered saline has been studied using dissolution calorimetry. The values of the reaction constant, the change in Gibbs energy, enthalpy, and entropy were obtained. It is shown that the ratio of the enthalpy and entropy factors depends on the charge of the peptide ion, and the number of H-bond acceptors in the peptide structure. The contributions of interaction between charged groups and polar fragments, hydrogen bonding, and stacking interaction are discussed, taking into account the effect of solvent reorganization around the reactant molecules.

Indexed as

beta-EndorphinTyrosineCytosineDipeptidesGlutathioneHumansPeptidesThermodynamicsUracilalanyltyrosinebeta-EndorphinCytosineDipeptidesGlutathionePeptidesTyrosineUracilalanyl tyrosinebeta-endorphin 30-31cytosineglutathionmolecular complexesthermodynamicsuracil

Identifiers

PMID37298713

DOI10.3390/ijms24119764

PMCPMC10253761

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.