Evidence map›Paper›PMID 40715733›Full record

ArticleEuropean biophysics journal : EBJ2026

In silico study of cytochrome-C binding to a cardiolipin-containing membrane.

Alessia Muroni, Fulvio Erba, Leonardo Domenichelli, Luisa Di Paola, Federica Sinibaldi, Giampiero Mei, Almerinda Di Venere, Velia Minicozzi

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2026. 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.

  1. 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

8 authors.

Alessia MuroniDepartment of Physics, University of Rome Tor Vergata, Via Della Ricerca Scientifica 1, 00133, Rome, Italy. alessia.muroni@roma2.infn.it.ORCID http://orcid.org/0009-0000-2141-1296
Fulvio ErbaDepartment of Clinical Science and Translational Medicine, Tor Vergata University of Rome, Via Montpellier 1, 00133, Rome, Italy.
Leonardo DomenichelliUnit of Chemical-Physics Fundamentals in Chemical Engineering, Department of Science and Technology for Sustainable Development and One Health, Università Campus Bio-Medico of Rome, 00128, Rome, Italy.
Luisa Di PaolaUnit of Chemical-Physics Fundamentals in Chemical Engineering, Department of Science and Technology for Sustainable Development and One Health, Università Campus Bio-Medico of Rome, 00128, Rome, Italy.
Federica SinibaldiDepartment of Clinical Science and Translational Medicine, Tor Vergata University of Rome, Via Montpellier 1, 00133, Rome, Italy.
Giampiero MeiDepartment of Experimental Medicine, University of Rome Tor Vergata, Via Montpellier 1, 00133, Rome, Italy.
Almerinda Di VenereDepartment of Experimental Medicine, University of Rome Tor Vergata, Via Montpellier 1, 00133, Rome, Italy.
Velia MinicozziDepartment of Physics, University of Rome Tor Vergata, Via Della Ricerca Scientifica 1, 00133, Rome, Italy. velia.minicozzi@uniroma2.it.

Funding

Ministero dell'Università e della Ricerca PROT.2022 PJKF88
6 · The paper itself

Abstract

Cytochrome C is a key protein involved in electron transport within the mitochondrial respiratory chain and in apoptosis mechanisms. In this work, we provide a detailed theoretical analysis of the binding mechanism between cytochrome-C and a cardiolipin-containing membrane. Molecular dynamics simulations, along with protein contact network and fractal dimension analyses were employed to investigate the structural changes in cytochrome-C during the binding process. Our results suggest that cytochrome-C follows a two-step binding mechanism, starting with a rapid initial interaction, followed by slower conformational rearrangements. We identified two different cytochrome-C conformations at the membrane: a compact, native-like structure and an extended form. The latter, stabilized by Lys72, exhibits a higher binding affinity (≈ 2 kcal/mol) compared to the former. Protein extension also correlates with increased protein-membrane contact and altered heme ring orientation, suggesting that the partial unfolding of cytochrome-C could be crucial for its peroxidase activity and its role in apoptosis. These findings enhance the understanding of the cytochrome-C's membrane interactions and its diverse functions.

Indexed as

CardiolipinsCell MembraneCytochromes cMolecular Dynamics SimulationProtein BindingProtein ConformationCardiolipinsCytochromes cCytochrome CFractal dimensionMembrane bindingProtein conformational dynamicsSuperficial roughness

Identifiers

PMID40715733
PMCPMC13109120

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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.