Activity and characterization of a pH-sensitive antimicrobial peptide

Hitchner, Morgan A.; Santiago-Ortiz, Luis E.; Necelis, Matthew R.; Shirley, David J.; Palmer, Thaddeus; Tarnawsky, Katharine; Vaden, Timothy D.; Caputo, Gregory A.

doi:10.1016/j.bbamem.2019.05.006

Cited by 40 publications

(33 citation statements)

References 75 publications

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“…The growth of bacteria in the positive control wells shows that there was no change in impact due to pH. Similar effects from pH changes on cationic peptide activity have been reported by other researchers [ 23 , 24 ]. Surprisingly, TS activity was substantially greater at pH 6.0 than pH 8.0, which shows that the antimicrobial activity of TS was a little higher under acidic conditions than basic conditions, although it maintained good antibacterial activity under a wide range of pH levels.…”

Section: Resultssupporting

confidence: 85%

Multiple Mechanisms of the Synthesized Antimicrobial Peptide TS against Gram-Negative Bacteria for High Efficacy Antibacterial Action In Vivo

et al. 2020

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The emergence of drug-resistant bacteria emphasizes the urgent need for novel antibiotics. The antimicrobial peptide TS shows extensive antibacterial activity in vitro and in vivo, especially in gram-negative bacteria; however, its antibacterial mechanism is unclear. Here, we find that TS without hemolytic activity disrupts the integrity of the outer bacterial cell membrane by displacing divalent cations and competitively binding lipopolysaccharides. In addition, the antimicrobial peptide TS can inhibit and kill E. coli by disintegrating the bacteria from within by interacting with bacterial DNA. Thus, antimicrobial peptide TS’s multiple antibacterial mechanisms may not easily induce bacterial resistance, suggesting use as an antibacterial drug to be for combating bacterial infections in the future.

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Section: Resultssupporting

confidence: 85%

Multiple Mechanisms of the Synthesized Antimicrobial Peptide TS against Gram-Negative Bacteria for High Efficacy Antibacterial Action In Vivo

et al. 2020

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“…This is consistent with previous reports that demonstrate cationic charge and net charge are important determinants of antimicrobial activity in AMPs. [ 41,54,60,61 ] These changes, however, do not appear to be driven by increased ability to permeabilize vesicles or native membranes. While increasing the net charge did result in moderate enhancements to lipid binding, this enhancement was not dependent on bilayer charge.…”

Section: Discussionmentioning

confidence: 98%

“…As the REES and TCE assays report on different aspects of Trp behavior (mobility and accessibility, respectively), the differences are potentially rooted in structural or aggregation state changes in the peptide in solution. [ 17,18,54 ] The CD spectra in Figure 6 indicate these three peptides (L1, L1‐Q, L1‐K) are not helical when in solution alone. However, the amino acid substitutions to change the net charge of the peptide are all at position 4, while the native Trp is at position 6 (Figure 1).…”

Section: Discussionmentioning

confidence: 99%

Investigation of the structure‐activity relationship in ponericin L1 from Neoponera goeldii

2020

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Naturally derived antimicrobial peptides have been an area of great interest because of high selectivity against bacterial targets over host cells and the limited development of bacterial resistance to these molecules throughout evolution. There are also a significant number of venom-derived peptides that exhibit antimicrobial activity in addition to activity against mammals or other organisms. Many venom peptides share the same net cationic, amphiphilic nature as host-defense peptides, making them an attractive target for development as potential antibacterial agents. The peptide ponericin L1 derived from Neoponera goeldii was used as a model to investigate the role of cationic residues and net charge on peptide activity. Using a combination of spectroscopic and microbiological approaches, the role of cationic residues and net charge on antibacterial activity, lipid bilayer interactions, and bilayer and membrane permeabilization were investigated. The L1 peptide and derivatives all showed enhanced binding to lipid vesicles containing anionic lipids, but still bound to zwitterionic vesicles. None of the derivatives were especially effective at permeabilizing lipid bilayers in model vesicles, in-tact Escherichia coli, or human red blood cells. Taken together the results indicate that the lack of facial amphiphilicity regarding charge segregation may impact the ability of the L1 peptides to effectively permeabilize bilayers despite effective binding. Additionally, increasing the net charge of the peptide by replacing the lone anionic residue with either Gln or Lys dramatically improved efficacy against several bacterial strains without increasing hemolytic activity. K E Y W O R D S antimicrobial peptides, fluorescence, lipid binding, membrane permeabilization, venom peptides

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“…The inactivation of the histidine-containing AMP C18G-His under low pH conditions involves pH-dependent changes in the state of the aggregates in the solution, because the aggregates, which are sensitive to pH and lipid composition, may be affected by binding and conformation. Peptides can also enhance bacterial membrane permeability at low pH ( Hitchner et al, 2019 ). Thrombin-derived C-terminal peptides (TCPs) will also change the mode of CD14 (a protein that is abundant in human plasma) from anti-inflammatory mode to bacterial elimination mode from pH 7.4 to pH 5.5 ( Holdbrook et al, 2018 ).…”

Section: Environmental Factors Affecting the Activity Of Antimicrobiamentioning

confidence: 99%

Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields

et al. 2020

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Antimicrobial peptides (AMPs) are a class of small peptides that widely exist in nature and they are an important part of the innate immune system of different organisms. AMPs have a wide range of inhibitory effects against bacteria, fungi, parasites and viruses. The emergence of antibiotic-resistant microorganisms and the increasing of concerns about the use of antibiotics resulted in the development of AMPs, which have a good application prospect in medicine, food, animal husbandry, agriculture and aquaculture. This review introduces the progress of research on AMPs comprehensively and systematically, including their classification, mechanism of action, design methods, environmental factors affecting their activity, application status, prospects in various fields and problems to be solved. The research progress on antivirus peptides, especially anti-coronavirus (COVID-19) peptides, has been introduced given the COVID-19 pandemic worldwide in 2020.

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Activity and characterization of a pH-sensitive antimicrobial peptide

Cited by 40 publications

References 75 publications

Multiple Mechanisms of the Synthesized Antimicrobial Peptide TS against Gram-Negative Bacteria for High Efficacy Antibacterial Action In Vivo

Multiple Mechanisms of the Synthesized Antimicrobial Peptide TS against Gram-Negative Bacteria for High Efficacy Antibacterial Action In Vivo

Investigation of the structure‐activity relationship in ponericin L1 from Neoponera goeldii

Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields

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