Antimicrobial activity and mechanism of peptide CM4 against Pseudomonas aeruginosa. Issue 8 (7th August 2020)
- Record Type:
- Journal Article
- Title:
- Antimicrobial activity and mechanism of peptide CM4 against Pseudomonas aeruginosa. Issue 8 (7th August 2020)
- Main Title:
- Antimicrobial activity and mechanism of peptide CM4 against Pseudomonas aeruginosa
- Authors:
- Li, Jian-Feng
Zhang, Jia-Xin
Li, Guo
Xu, Yan-Yan
Lu, Kai
Wang, Zhi-Guo
Liu, Jun-Ping - Abstract:
- Abstract : Amidated peptide CM4 showed good activity in in vitro bacteriostasis experiments and may be used as a novel food preservative. Abstract : Antibacterial peptide CM4 (ABP-CM4) is a small cationic peptide with broad-spectrum activities against bacteria, fungi and tumor cells and may possibly be used as an antimicrobial agent. In this study, a C-terminal amidated antibacterial peptide ABP-CM4 (ABP-CM4N) with the strongest antibacterial activity was obtained through screening the antibacterial activities of ABP-CM4 with different modifications. The minimal inhibitory concentration of ABP-CM4N was 8 μM against P. aeruginosa (ATCC 27853) which was lower than that of ABP-CM4 (16 μM). The strengthened antimicrobial activity of ABP-CM4N may be associated with the increased membrane binding capacity, being two times that of ABP-CM4 ( p < 0.001). The antibacterial mechanism of ABP-CM4N to Pseudomonas aeruginosa was examined by means of cell membrane integrity analysiss, the intracellular ultrastructure change observation and E. coli genomic DNA binding assay. It was found that ABP-CM4N had the same antimicrobial mechanism as ABP-CM4, and the aim of the antimicrobial mechanism was mainly to destroy the cell membrane which caused nucleic acid or protein leakage, and secondly to interact with E. coli genomic DNA after penetrating the cell membrane. Furthermore, in vitro ABP-CM4N showed a better bacteriostatic activity in meats, with the treated samples showing two to three timesAbstract : Amidated peptide CM4 showed good activity in in vitro bacteriostasis experiments and may be used as a novel food preservative. Abstract : Antibacterial peptide CM4 (ABP-CM4) is a small cationic peptide with broad-spectrum activities against bacteria, fungi and tumor cells and may possibly be used as an antimicrobial agent. In this study, a C-terminal amidated antibacterial peptide ABP-CM4 (ABP-CM4N) with the strongest antibacterial activity was obtained through screening the antibacterial activities of ABP-CM4 with different modifications. The minimal inhibitory concentration of ABP-CM4N was 8 μM against P. aeruginosa (ATCC 27853) which was lower than that of ABP-CM4 (16 μM). The strengthened antimicrobial activity of ABP-CM4N may be associated with the increased membrane binding capacity, being two times that of ABP-CM4 ( p < 0.001). The antibacterial mechanism of ABP-CM4N to Pseudomonas aeruginosa was examined by means of cell membrane integrity analysiss, the intracellular ultrastructure change observation and E. coli genomic DNA binding assay. It was found that ABP-CM4N had the same antimicrobial mechanism as ABP-CM4, and the aim of the antimicrobial mechanism was mainly to destroy the cell membrane which caused nucleic acid or protein leakage, and secondly to interact with E. coli genomic DNA after penetrating the cell membrane. Furthermore, in vitro ABP-CM4N showed a better bacteriostatic activity in meats, with the treated samples showing two to three times less positive colonies than ABP-CM4. … (more)
- Is Part Of:
- Food & function. Volume 11:Issue 8(2020)
- Journal:
- Food & function
- Issue:
- Volume 11:Issue 8(2020)
- Issue Display:
- Volume 11, Issue 8 (2020)
- Year:
- 2020
- Volume:
- 11
- Issue:
- 8
- Issue Sort Value:
- 2020-0011-0008-0000
- Page Start:
- 7245
- Page End:
- 7254
- Publication Date:
- 2020-08-07
- Subjects:
- Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
Nutrition -- Periodicals
664.07 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/FO ↗
http://pubs.rsc.org/en/journals/journal/fo ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d0fo01031f ↗
- Languages:
- English
- ISSNs:
- 2042-6496
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.038457
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 13888.xml