Evidence map›Paper›PMID 40943647›Full record

ArticleInternational journal of molecular sciences2025

Lignin-Derived Oligomers as Promising mTOR Inhibitors: Insights from Dynamics Simulations.

Sofia Gabellone, Giovanni Carotenuto, Manuel Arcieri, Paolo Bottoni, Giulia Sbanchi, Tiziana Castrignanò, Davide Piccinino, Chiara Liverani, Raffaele Saladino

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

9 authors.

Sofia GabelloneIRCCS Istituto Romagnolo per lo Studio dei Tumori "Dino Amadori"-IRST Srl, 47014 Meldola, Italy.ORCID 0000-0003-1311-3082
Giovanni CarotenutoDepartment of Ecological and Biological Sciences, Tuscia University, Viale dell'Università s.n.c., 01100 Viterbo, Italy.ORCID 0009-0007-5328-4683
Manuel ArcieriDepartment of Computer Science, "Sapienza" University of Rome, V. le Regina Elena 295, 00161 Rome, Italy.ORCID 0000-0002-2312-7704
Paolo BottoniDepartment of Computer Science, "Sapienza" University of Rome, V. le Regina Elena 295, 00161 Rome, Italy.ORCID 0000-0003-4662-2019
Giulia SbanchiIRCCS Istituto Romagnolo per lo Studio dei Tumori "Dino Amadori"-IRST Srl, 47014 Meldola, Italy.ORCID 0009-0004-6141-1572
Tiziana CastrignanòDepartment of Ecological and Biological Sciences, Tuscia University, Viale dell'Università s.n.c., 01100 Viterbo, Italy.ORCID 0000-0002-0689-6720
Davide PiccininoDepartment of Ecological and Biological Sciences, Tuscia University, Viale dell'Università s.n.c., 01100 Viterbo, Italy.ORCID 0000-0002-6561-2222
Chiara LiveraniIRCCS Istituto Romagnolo per lo Studio dei Tumori "Dino Amadori"-IRST Srl, 47014 Meldola, Italy.ORCID 0000-0002-4279-1926
Raffaele SaladinoDepartment of Ecological and Biological Sciences, Tuscia University, Viale dell'Università s.n.c., 01100 Viterbo, Italy.ORCID 0000-0002-4420-9063

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mammalian target of rapamycin pathway, mTOR, is a crucial signaling pathway that regulates cell growth, proliferation, metabolism, and survival. Due to its dysregulation it is involved in several ailments such as cancer or age-related diseases. The discovery of mTOR and the understanding of its biological functions were greatly facilitated by the use of rapamycin, an antibiotic of natural origin, which allosterically inhibits mTORC1, effectively blocking its function. In this entirely computational study, we investigated mTOR's interaction with seven ligands: two clinically established inhibitors (everolimus and rapamycin) and five lignin-derived oligomers, a renewable natural polyphenol recently used for the drug delivery of everolimus. The seven complexes were analyzed through all-atom molecular dynamics simulations in explicit solvent using a high-performance computing platform. Trajectory analyses revealed stable interactions between mTOR and all ligands, with lignin-derived compounds showing comparable or enhanced binding stability relative to reference drugs. To evaluate the stability of the molecular complex and the behavior of the ligand over time, we analyzed key parameters including root mean square deviation, root mean square fluctuation, number of hydrogen bonds, binding free energy, and conformational dynamics assessed through principal component analysis. Our results suggest that lignin fragments are a promising, sustainable scaffold for developing novel mTOR inhibitors.

Indexed as

LigninMolecular Dynamics SimulationMTOR InhibitorsTOR Serine-Threonine KinasesEverolimusHumansHydrogen BondingLigandsMolecular Docking SimulationProtein BindingSirolimusEverolimusLigandsLigninMTOR InhibitorsSirolimusTOR Serine-Threonine Kinaseseverolimushigh-performance computing (HPC)hydrophobic and hydrogen bond interactionslignin-derived oligomersMM/PBSA binding free energymolecular dynamics (MD) simulationsmTORmTOR inhibitorsrapamycin

Identifiers

PMID40943647
PMCPMC12429072

What Socratic 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 Socratic graph.