Next Article in Journal
1,2,6-Thiadiazinones as Novel Narrow Spectrum Calcium/Calmodulin-Dependent Protein Kinase Kinase 2 (CaMKK2) Inhibitors
Previous Article in Journal
Targeting Protein Quality Control Mechanisms by Natural Products to Promote Healthy Ageing
Open AccessArticle

Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity against Human Cells of a Peptide Derived from Bovine αS1-Casein

1
Key Laboratory of Dairy Science, Northeast Agricultural University, College of Food Science, Harbin 150030, China
2
Harbin Veterinary Research Institute, CAAS, Harbin 150001, China
*
Author to whom correspondence should be addressed.
Molecules 2018, 23(5), 1220; https://doi.org/10.3390/molecules23051220
Received: 18 April 2018 / Revised: 5 May 2018 / Accepted: 17 May 2018 / Published: 19 May 2018
The primary objective of this study was to improve our understanding of the antimicrobial mechanism of protein-derived peptides and to provide evidence for protein-derived peptides as food bio-preservatives by examining the antimicrobial activities, low cytotoxicity, stabilities, and mechanism of Cp1 (LRLKKYKVPQL). In this study, the protein-derived peptide Cp1 was synthesized from bovine αS1-casein, and its potential use as a food biopreservative was indicated by the higher cell selectivity shown by 11-residue peptide towards bacterial cells than human RBCs. It also showed broad-spectrum antimicrobial activity, with minimum inhibitory concentrations (MICs) of 64–640 μM against both gram-positive and gram-negative bacteria. The peptide had low hemolytic activity (23.54%, 512 μM) as well as cytotoxicity. The results of fluorescence spectroscopy, flow cytometry, and electron microscopy experiments indicated that Cp1 exerted its activity by permeabilizing the microbial membrane and destroying cell membrane integrity. We found that Cp1 had broad-spectrum antimicrobial activity, low hemolytic activity, and cytotoxicity. The results also revealed that Cp1 could cause cell death by permeabilizing the cell membrane and disrupting membrane integrity. Overall, the findings presented in this study improve our understanding of the antimicrobial potency of Cp1 and provided evidence of the antimicrobial mechanisms of Cp1. The peptide Cp1 could have potential applications as a food biopreservative. View Full-Text
Keywords: antibacterial peptides; antimicrobial activity; hemolytic activity; human cell; cytotoxicity mechanism antibacterial peptides; antimicrobial activity; hemolytic activity; human cell; cytotoxicity mechanism
Show Figures

Graphical abstract

MDPI and ACS Style

Hou, J.; Liu, Z.; Cao, S.; Wang, H.; Jiang, C.; Hussain, M.A.; Pang, S. Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity against Human Cells of a Peptide Derived from Bovine αS1-Casein. Molecules 2018, 23, 1220. https://doi.org/10.3390/molecules23051220

AMA Style

Hou J, Liu Z, Cao S, Wang H, Jiang C, Hussain MA, Pang S. Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity against Human Cells of a Peptide Derived from Bovine αS1-Casein. Molecules. 2018; 23(5):1220. https://doi.org/10.3390/molecules23051220

Chicago/Turabian Style

Hou, Juncai; Liu, Zhijing; Cao, Songsong; Wang, Haimei; Jiang, Chenggang; Hussain, Muhammad A.; Pang, Shiyue. 2018. "Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity against Human Cells of a Peptide Derived from Bovine αS1-Casein" Molecules 23, no. 5: 1220. https://doi.org/10.3390/molecules23051220

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop