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Temporin-Like Peptides Show Antimicrobial and Anti-Biofilm Activities against Streptococcus mutans with Reduced Hemolysis.


ABSTRACT: In our previous study, temporin-GHaR (GHaR) showed potent antimicrobial activity with strong hemolytic toxicity. To overcome its weakness, we designed GHaR6R, GHaR7R, GHaR8R, GHaR9R, and GHaR9W by changing the number of positive charges and the hydrophobic surface of GHaR. With the exception of GHaR7R, the hemolytic toxicity of the derived peptides had been reduced, and the antimicrobial activities remained close to the parent peptide (except for GHaR9R). GHaR6R, GHaR7R, GHaR8R, and GHaR9W exhibited a great bactericidal effect on Streptococcus mutans (S. mutans), which is one of the main pathogens causing dental caries. According to the membrane permeation and scanning electron microscope (SEM) analysis, these derived peptides targeted to the cell membranes of planktonic bacteria, contributing to the disruption of the membrane integrity and leakage of the intracellular contents. Moreover, they inhibited the formation of biofilms and eradicated the mature biofilms of S. mutans. Compared with GHaR7R, the derived peptides showed less cytotoxicity to human oral epithelial cells (HOECs). The derived peptides are expected to be the molecular templates for designing antibacterial agents to prevent dental caries.

SUBMITTER: Wei H 

PROVIDER: S-EPMC7730238 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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Temporin-Like Peptides Show Antimicrobial and Anti-Biofilm Activities against <i>Streptococcus mutans</i> with Reduced Hemolysis.

Wei Hanqi H   Xie Zhipeng Z   Tan Xiuchuan X   Guo Ran R   Song Yanting Y   Xie Xi X   Wang Rong R   Li Lushuang L   Wang Manchuriga M   Zhang Yingxia Y  

Molecules (Basel, Switzerland) 20201204 23


In our previous study, temporin-GHaR (GHaR) showed potent antimicrobial activity with strong hemolytic toxicity. To overcome its weakness, we designed GHaR6R, GHaR7R, GHaR8R, GHaR9R, and GHaR9W by changing the number of positive charges and the hydrophobic surface of GHaR. With the exception of GHaR7R, the hemolytic toxicity of the derived peptides had been reduced, and the antimicrobial activities remained close to the parent peptide (except for GHaR9R). GHaR6R, GHaR7R, GHaR8R, and GHaR9W exhib  ...[more]

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