دورية أكاديمية
Structural and Functional Characterization of a Novel Recombinant Antimicrobial Peptide from Hermetia illucens
| العنوان: | Structural and Functional Characterization of a Novel Recombinant Antimicrobial Peptide from Hermetia illucens |
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| المؤلفون: | Angela Di Somma, Antonio Moretta, Carolina Cané, Carmen Scieuzo, Rosanna Salvia, Patrizia Falabella, Angela Duilio |
| المصدر: | Current Issues in Molecular Biology, Vol 44, Iss 1, Pp 1-13 (2021) |
| بيانات النشر: | MDPI AG, 2021. |
| سنة النشر: | 2021 |
| المجموعة: | LCC:Biology (General) |
| مصطلحات موضوعية: | antimicrobial peptides, defensins, insects, Hermetia illucens, antibacterial activity, Biology (General), QH301-705.5 |
| الوصف: | Antibiotics are commonly used to treat pathogenic bacteria, but their prolonged use contributes to the development and spread of drug-resistant microorganisms raising the challenge to find new alternative drugs. Antimicrobial peptides (AMPs) are small/medium molecules ranging 10–60 residues synthesized by all living organisms and playing important roles in the defense systems. These features, together with the inability of microorganisms to develop resistance against the majority of AMPs, suggest that these molecules might represent effective alternatives to classical antibiotics. Because of their high biodiversity, with over one million described species, and their ability to live in hostile environments, insects represent the largest source of these molecules. However, production of insect AMPs in native forms is challenging. In this work we investigate a defensin-like antimicrobial peptide identified in the Hermetia illucens insect through a combination of transcriptomics and bioinformatics approaches. The C-15867 AMP was produced by recombinant DNA technology as a glutathione S-transferase (GST) fusion peptide and purified by affinity chromatography. The free peptide was then obtained by thrombin proteolysis and structurally characterized by mass spectrometry and circular dichroism analyses. The antibacterial activity of the C-15867 peptide was evaluated in vivo by determination of the minimum inhibitory concentration (MIC). Finally, crystal violet assays and SEM analyses suggested disruption of the cell membrane architecture and pore formation with leaking of cytosolic material. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 44010001 1467-3045 1467-3037 |
| Relation: | https://www.mdpi.com/1467-3045/44/1/1; https://doaj.org/toc/1467-3037; https://doaj.org/toc/1467-3045 |
| DOI: | 10.3390/cimb44010001 |
| URL الوصول: | https://doaj.org/article/76c056f23e2d4c9d8a8a15c4e7f48bb9 |
| رقم الأكسشن: | edsdoj.76c056f23e2d4c9d8a8a15c4e7f48bb9 |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 44010001 14673045 14673037 |
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| DOI: | 10.3390/cimb44010001 |