Evidence map›Paper›PMID 40221471›Full record

ArticleScientific reports2025

Elucidating the synergistic role of hybrid peptide from Burkholderia cepacia enzymes in biodegradation of polycyclic aromatic hydrocarbons.

Muhammad Naveed, Ayesha Saleem, Tariq Aziz, Khadija Khatoon, Maida Salah Ud Din, Ahiba Adil, Mitub Al-Harbi, Abdullah F Alasmari

Abstract read
In one paragraph

Article in Scientific reports, 2025. 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.

Muhammad NaveedDepartment of Biotechnology, Faculty of Science and Technology, University of Central Punjab, Lahore, 54590, Pakistan. naveed.quadian@gmail.com.
Ayesha SaleemDepartment of Biotechnology, Faculty of Science and Technology, University of Central Punjab, Lahore, 54590, Pakistan.
Tariq AzizLaboratory of Animal Health Food Hygiene and Quality, Department of Agriculture, University of Ioannina, Arta, Greece. iwockd@gmail.com.
Khadija KhatoonDepartment of Biotechnology, Faculty of Science and Technology, University of Central Punjab, Lahore, 54590, Pakistan.
Maida Salah Ud DinDepartment of Biotechnology, Faculty of Science and Technology, University of Central Punjab, Lahore, 54590, Pakistan.
Ahiba AdilDepartment of Biotechnology, Faculty of Science and Technology, University of Central Punjab, Lahore, 54590, Pakistan.
Mitub Al-HarbiDepartment of Pharmacology and Toxicology College of Pharmacy, King Saud University, Riyadh, Saudi Arabia.
Abdullah F AlasmariDepartment of Pharmacology and Toxicology College of Pharmacy, King Saud University, Riyadh, Saudi Arabia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polycyclic aromatic hydrocarbons (PAHs) are hazardous environmental contaminants emerging from industrial activities and fossil fuel combustion, posing risks to human health and ecosystems. Biodegradation offers a sustainable approach to mitigating PAH pollution, and here we investigated the efficacy of a peptide hybrid of laccase and O-methyltransferase enzymes from the bacterium Burkholderia cepacia in PAH degradation. Both enzymes demonstrated stability with an instability index below 40, indicating suitability for environmental application. Following active site prediction, the 3D structure of the peptide hybrid, consisting of 71 amino acids, was modelled using trRosetta, achieving a high-quality structure with an ERRAT score above 97%. Further bioinformatic analysis confirmed the hybrid's non-allergenic and non-virulent properties. Molecular docking studies revealed a robust binding affinity above - 9 kcal/mol, highlighting this peptide hybrid's potential for effective PAH degradation and suggesting its promise as an eco-friendly bioremediation agent for PAH-contaminated sites.

Indexed as

Bacterial ProteinsBurkholderia cepaciaLaccaseMethyltransferasesPeptidesPolycyclic Aromatic HydrocarbonsBiodegradation, EnvironmentalCatalytic DomainMolecular Docking SimulationBacterial ProteinsLaccaseMethyltransferasesPeptidesPolycyclic Aromatic HydrocarbonsBioremediationLaccaseMolecular DockingO-methyltransferasePAHs degradationPeptide

Identifiers

PMID40221471
PMCPMC11993559

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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.