Naveed Muhammad, Saleem Ayesha, Aziz Tariq, Khatoon Khadija, Din Maida Salah Ud, Adil Ahiba, Al-Harbi Mitub, Alasmari Abdullah F
Department of Biotechnology, Faculty of Science and Technology, University of Central Punjab, Lahore, 54590, Pakistan.
Laboratory of Animal Health Food Hygiene and Quality, Department of Agriculture, University of Ioannina, Arta, Greece.
Sci Rep. 2025 Apr 12;15(1):12603. doi: 10.1038/s41598-025-97007-1.
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.
多环芳烃（PAHs）是由工业活动和化石燃料燃烧产生的有害环境污染物，对人类健康和生态系统构成风险。生物降解为减轻PAH污染提供了一种可持续的方法，在此我们研究了来自洋葱伯克霍尔德菌的漆酶和O-甲基转移酶的肽杂合体在PAH降解中的功效。两种酶均表现出稳定性，不稳定指数低于40，表明适用于环境应用。在活性位点预测之后，使用trRosetta对由71个氨基酸组成的肽杂合体的三维结构进行建模，获得了ERRAT分数高于97%的高质量结构。进一步的生物信息学分析证实了该杂合体的无致敏性和无毒性特性。分子对接研究揭示了高于-9千卡/摩尔的强大结合亲和力，突出了这种肽杂合体有效降解PAH的潜力，并表明其有望成为用于PAH污染场地的生态友好型生物修复剂。
