Safety and Antibacterial Mechanism of Bovine Lactoferrin Derived Peptide FP-PF

被引:0
|
作者
Fu Y. [1 ]
Li Y. [1 ]
Jiang Z. [1 ]
Liu F. [1 ]
Jiang C. [2 ]
Hou J. [1 ]
Tian B. [1 ]
Wang Y. [1 ]
机构
[1] College of Food Science, Northeast Agricultural University, Harbin
[2] Harbin Veterinary Research Institute, CAAS, Harbin
关键词
Antibacterial mechanism; Antibacterial peptide; Cytotoxicity; Hemolysis activity;
D O I
10.16429/j.1009-7848.2020.08.011
中图分类号
学科分类号
摘要
Lactoferrin is a unique ingredient in milk, which has the functions of broad-spectrum antibacterial, anti-inflammatory, inhibition of tumor cell growth and regulation of immune response. It is a new antimicrobial and anticancer component. In this experiment, the new antimicrobial peptide FP-PF was designed with the idea of a symmetrical structure as the basis, and melittin was used as the positive control peptide. The cytotoxicity, hemolytic activity and bacteriostatic mechanism of the new antimicrobial peptides FP-PF were studied. The experimental results showed that the hemolysis rate of FP-PF which concentation was at the range of 1-256 mmol/L was less than 5%, indicating that the hemolysis rate was low. The cell survival rate was more than 92%, indicating that its cytotoxicity was small. Through the study of bacteriostatic mechanism, the antibacterial peptide FP-PF could damage the outer and inner membranes of cell membranes, change its osmotic pressure and integrity, and thus achieve the effect of sterilization and bacteriostasis. Therefore, the new antimicrobial peptide FP-PF designed in this experiment was expected to show its potential application value in food, cosmetics and so on. © 2020, Editorial Office of Journal of CIFST. All right reserved.
引用
收藏
页码:92 / 99
页数:7
相关论文
共 24 条
  • [1] GUAN Y D, WANG B, GAO Y X, Et al., Occurrence and fate of antibiotics in the aqueous environment and their removal by constructed wetlands in China: a review, Pedosphere, 27, 1, pp. 42-51, (2017)
  • [2] 3, pp. 5-9
  • [3] 7
  • [4] 5
  • [5] 10
  • [6] GIACOMETTI A, CIRIONI O, KAMYSZ W, Et al., Comparative activities of cecropin A, melittin, and cecropin A-melittin peptide CA(1-7)M(2-9)NH2 against multidrug-resistant nosocomial isolates of Acinetobacter baumannii, Peptides, 24, 9, pp. 1315-1318, (2003)
  • [7] ZWEYTICK D, DEUTSCH G, ANDRA J, Et al., Studies on lactoferricin-derived Escherichia coli membrane-active peptides reveal differences in the mechanism of N-acylated versus nonacylated peptides, Journal of Biological Chemistry, 286, 24, pp. 21266-21276, (2011)
  • [8] SANCHEZ-GOMEZ S, FERRER-ESPADA R, STEWART P S, Et al., Antimicrobial activity of synthetic cationic peptides and lipopeptides derived from human lactoferricin against Pseudomonas aeruginosa planktonic cultures and biofilms, BMC Microbiology, 15, 1, pp. 132-137, (2015)
  • [9] MA Q Q, DONG N, SHAN A S, Et al., Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units, Amino acids, 43, 6, pp. 2527-2536, (2012)
  • [10] ZHOU N, TIELEMAN D P, VOGEL H J., Molecular dynamics simulations of bovine lactoferricin: turning a helix into a sheet, Biometals, 17, 3, pp. 217-223, (2004)