scholarly journals The antimicrobial effects of the alginate oligomer OligoG CF-5/20 are independent of direct bacterial cell membrane disruption

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Manon F. Pritchard ◽  
Lydia C. Powell ◽  
Saira Khan ◽  
Peter C. Griffiths ◽  
Omar T. Mansour ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Bacterial Cell ◽  
Membrane Disruption ◽  
Antimicrobial Effects ◽  
Cell Membrane Disruption ◽  
Bacterial Cell Membrane

scholarly journals Novel Antimicrobial Peptides from a Cecropin-Like Region of Heteroscorpine-1 from Heterometrus laoticus Venom with Membrane Disruption Activity

Molecules ◽  
2021 ◽  
Vol 26 (19) ◽  
pp. 5872
Author(s):  
Rima Erviana ◽  
Yutthakan Saengkun ◽  
Prapenpuksiri Rungsa ◽  
Nisachon Jangpromma ◽  
Patcharaporn Tippayawat ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Membrane ◽  
Antimicrobial Peptides ◽  
Bacterial Cell ◽  
Sem Analysis ◽  
Membrane Disruption ◽  
Amino Acid Residues ◽  
Bacterial Strains ◽  
Charged Amino Acids ◽  
Bacterial Cell Membrane

The increasing antimicrobial-resistant prevalence has become a severe health problem. It has led to the invention of a new antimicrobial agent such as antimicrobial peptides. Heteroscorpine-1 is an antimicrobial peptide that has the ability to kill many bacterial strains. It consists of 76 amino acid residues with a cecropin-like region in N-terminal and a defensin-like region in the C-terminal. The cecropin-like region from heteroscorpine-1 (CeHS-1) is similar to cecropin B, but it lost its glycine-proline hinge region. The bioinformatics prediction was used to help the designing of mutant peptides. The addition of glycine-proline hinge and positively charged amino acids, the deletion of negatively charged amino acids, and the optimization of the hydrophobicity of the peptide resulted in two mutant peptides, namely, CeHS-1 GP and CeHS-1 GPK. The new mutant peptide showed higher antimicrobial activity than the native peptide without increasing toxicity. The interaction of the peptides with the membrane showed that the peptides were capable of disrupting both the inner and outer bacterial cell membrane. Furthermore, the SEM analysis showed that the peptides created the pore in the bacterial cell membrane resulted in cell membrane disruption. In conclusion, the mutants of CeHS-1 had the potential to develop as novel antimicrobial peptides.

Design of bio-molecular interfaces using liquid crystals demonstrating endotoxin interactions with bacterial cell wall components

RSC Advances ◽  
2015 ◽  
Vol 5 (81) ◽  
pp. 66476-66486 ◽  
Author(s):  
Dibyendu Das ◽  
Sumyra Sidiq ◽  
Santanu Kumar Pal
Keyword(s):  
Cell Wall ◽  
Liquid Crystals ◽  
Cell Membrane ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Cell Wall Components ◽  
Bacterial Cell Membrane ◽  
Membrane Components ◽  
Wall Components

Liquid crystals offer a promising approach to study and quantify the interactions between different bacterial cell membrane components with endotoxin at an aqueous interface.

scholarly journals Telavancin, a Multifunctional Lipoglycopeptide, Disrupts both Cell Wall Synthesis and Cell Membrane Integrity in Methicillin-Resistant Staphylococcus aureus

2005 ◽  
Vol 49 (3) ◽  
pp. 1127-1134 ◽  
Author(s):  
Deborah L. Higgins ◽  
Ray Chang ◽  
Dmitri V. Debabov ◽  
Joey Leung ◽  
Terry Wu ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Membrane Potential ◽  
Cell Membrane ◽  
Bactericidal Activity ◽  
Bacterial Cell ◽  
Cell Membrane Potential ◽  
Gram Positive ◽  
Methicillin Resistant ◽  
Bacterial Cell Membrane

ABSTRACTThe emergence and spread of multidrug-resistant gram-positive bacteria represent a serious clinical problem. Telavancin is a novel lipoglycopeptide antibiotic that possesses rapid in vitro bactericidal activity against a broad spectrum of clinically relevant gram-positive pathogens. Here we demonstrate that telavancin's antibacterial activity derives from at least two mechanisms. As observed with vancomycin, telavancin inhibited late-stage peptidoglycan biosynthesis in a substrate-dependent fashion and bound the cell wall, as it did the lipid II surrogate tripeptideN,N′-diacetyl-l-lysinyl-d-alanyl-d-alanine, with high affinity. Telavancin also perturbed bacterial cell membrane potential and permeability. In methicillin-resistantStaphylococcus aureus, telavancin caused rapid, concentration-dependent depolarization of the plasma membrane, increases in permeability, and leakage of cellular ATP and K+. The timing of these changes correlated with rapid , concentration-dependent loss of bacterial viability, suggesting that the early bactericidal activity of telavancin results from dissipation of cell membrane potential and an increase in membrane permeability. Binding and cell fractionation studies provided direct evidence for an interaction of telavancin with the bacterial cell membrane; stronger binding interactions were observed with the bacterial cell wall and cell membrane relative to vancomycin. We suggest that this multifunctional mechanism of action confers advantageous antibacterial properties.

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