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The Recombinant Production of Novel Bovine Lactoferricin Engineered Peptide Using Molecular Dynamic Simulation | ||
| Archives of Razi Institute | ||
| مقالات آماده انتشار، پذیرفته شده، انتشار آنلاین از تاریخ 21 آبان 1403 اصل مقاله (414.27 K) | ||
| نوع مقاله: Original Articles | ||
| شناسه دیجیتال (DOI): 10.22092/ari.2024.364695.3006 | ||
| نویسندگان | ||
| Maryam Akbari Azam1؛ Abbas Ali Motalebi2؛ Mohammadreaza Nassiri* 3؛ Amir Ali Anvar4 | ||
| 1Department of Food Hygiene, Science and Research Branch, Islamic Azad University, Tehran. Iran | ||
| 2Department of food Hygiene, Science and Research Branch, Islamic Azad University, Tehran, Iran | ||
| 3Faculty of agriculture, Ferdowsi university of Mashhad, Iran | ||
| 4Department of Food Hygiene, Science and Research Branch, Islamic Azad University, Tehran, Iran | ||
| چکیده | ||
| Antimicrobial peptides (AMPs) are native and safe short peptides that are considered one of the best alternatives for antibiotics. Although numerous studies have been conducted on AMPs, their mode of action has not yet been fully understood. Computational peptide engineering can provide valuable insight into the stability and potency of AMPs against targets. In the present study, we performed a molecular dynamics simulation study to understand the mode of action of Bovine Lfcin and to improve the interactions between Bovine Lfcin (wild and mutant types) and DNA (an important intracellular target), DNAK (an important protein in pathogenicity, mostly in gram-negative bacteria), and LysM (an important surface protein in gram-positive bacteria). The nucleotide sequence of Lfcin peptide was synthesized and cloned in pET22b (+). Induction of gene expression was done using 1mM IPTG and recombinant peptide was purified using His-tag marker. The antimicrobial peptide activity was performed on Escherichia coli O157 and Bacillus subtilis Gram- negative and positive bacteria using disk diffusion methods, respectively. Our results showed that all the changes in Bovine Lfcin wild type observed in this study improved the peptide-DNA, DNAK, and LysM interactions. Based on the results, removing the PHE25 residue from the wild type Bovine Lfcin peptide had more significant effects on complex formation with DNA, DNAK, and LysM. The recombinant production of a Lfcin peptide with a molecular weight of ~5 KDa was confirmed by SDS PAGE. The performance of Lfcin peptide on pathogenic bacteria was strong and it had the strongest effect in concentrations of 6 and 8 mg/ml for gram positive and negative bacteria, respectively. | ||
| کلیدواژه‌ها | ||
| Antimicrobial peptides, Bovine Lfcin؛ Recombinant Protein | ||
| عنوان مقاله [English] | ||
| تولید نوترکیب پپتید ضدمیکروبی مهندسی شده لاکتوفرسین با استفاده از محاسبات دینامیک مولکلولی | ||
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