Characterization of antibacterial activity and mechanisms of two linear derivatives of bactenecin. (June 2019)
- Record Type:
- Journal Article
- Title:
- Characterization of antibacterial activity and mechanisms of two linear derivatives of bactenecin. (June 2019)
- Main Title:
- Characterization of antibacterial activity and mechanisms of two linear derivatives of bactenecin
- Authors:
- Liu, Fei
Wang, Haimei
Cao, Songsong
Jiang, Chenggang
Hou, Juncai - Abstract:
- Abstract: Antibiotic resistance is a significant global healthcare issue, and the development of alternative classes of antimicrobial agents with new modes of action is therefore critical. In the current study, two derivatives of the antimicrobial peptide bactenecin which were Bac2a, a 12-residue peptide, and Bac8c, an 8-residue peptide were synthesized, then their antimicrobial properties, stabilities, and mechanisms of action were investigated. Results showed that the minimum inhibitory concentrations (MICs) of Bac2a against gram-negative and gram-positive bacteria ranged from 2 to 32 μM, while Bac8c exhibited greater antimicrobial activity with MICs ranging from 2 to 16 μM Bac8c also exhibited lower hemolytic and cytotoxic activities compared with those of Bac2a. The antibacterial activities of the peptides were not inhibited by heat, and Bac8c possessed a higher antibacterial activity in the presence of salts and enzymes. Fluorescence spectroscopy, flow cytometry, and scanning and transmission electron microscopy indicated that Bac8c exhibited high antimicrobial potency by inducing cytoplasmic membrane potential loss, as well as membrane permeabilization and disruption. Based on the results of the analyses, Bac8c represents a promising candidate for novel antimicrobial applications. Highlights: Two derivatives of antimicrobial peptide bactenecin which were Bac2a and Bac8c were synthesized and characterized. Bac2a and Bac8c had strong thermal stability, and Bac8cAbstract: Antibiotic resistance is a significant global healthcare issue, and the development of alternative classes of antimicrobial agents with new modes of action is therefore critical. In the current study, two derivatives of the antimicrobial peptide bactenecin which were Bac2a, a 12-residue peptide, and Bac8c, an 8-residue peptide were synthesized, then their antimicrobial properties, stabilities, and mechanisms of action were investigated. Results showed that the minimum inhibitory concentrations (MICs) of Bac2a against gram-negative and gram-positive bacteria ranged from 2 to 32 μM, while Bac8c exhibited greater antimicrobial activity with MICs ranging from 2 to 16 μM Bac8c also exhibited lower hemolytic and cytotoxic activities compared with those of Bac2a. The antibacterial activities of the peptides were not inhibited by heat, and Bac8c possessed a higher antibacterial activity in the presence of salts and enzymes. Fluorescence spectroscopy, flow cytometry, and scanning and transmission electron microscopy indicated that Bac8c exhibited high antimicrobial potency by inducing cytoplasmic membrane potential loss, as well as membrane permeabilization and disruption. Based on the results of the analyses, Bac8c represents a promising candidate for novel antimicrobial applications. Highlights: Two derivatives of antimicrobial peptide bactenecin which were Bac2a and Bac8c were synthesized and characterized. Bac2a and Bac8c had strong thermal stability, and Bac8c exhibited higher stability against salts and enzymes treatments. Bac8c exhibited high antimicrobial potency by inducing cell membrane potential loss, permeabilization and disruption. … (more)
- Is Part Of:
- Lebensmittel-Wissenschaft + Technologie =. Volume 107(2019)
- Journal:
- Lebensmittel-Wissenschaft + Technologie =
- Issue:
- Volume 107(2019)
- Issue Display:
- Volume 107, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 107
- Issue:
- 2019
- Issue Sort Value:
- 2019-0107-2019-0000
- Page Start:
- 89
- Page End:
- 97
- Publication Date:
- 2019-06
- Subjects:
- Bactenecin -- Peptides -- Antibacterial activity -- Mechanism of action -- Stability
Food industry and trade -- Periodicals
Food -- Composition -- Periodicals
Microbiology -- Periodicals
Nutrition -- Periodicals
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00236438 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.lwt.2019.02.073 ↗
- Languages:
- English
- ISSNs:
- 0023-6438
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3983.070000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 9830.xml