Differential presentation of a single antimicrobial peptide is sufficient to identify LPS from distinct bacterial samples

The Analyst ◽  
2019 ◽  
Vol 144 (24) ◽  
pp. 7242-7249 ◽  
Author(s):  
Timothy M. Reichart ◽  
Joshua R. Uzarski ◽  
Charlene M. Mello
Keyword(s):  
Antimicrobial Peptide ◽  
Gram Negative Bacteria ◽  
Site Specific ◽  
Gram Negative

Site-specific immobilization of an antimicrobial peptide permits the sensing and identification of lipopolysaccharide samples from a range of Gram-negative bacteria.

scholarly journals Interaction of Antimicrobial Peptide Temporin L with Lipopolysaccharide In Vitro and in Experimental Rat Models of Septic Shock Caused by Gram-Negative Bacteria

2006 ◽  
Vol 50 (7) ◽  
pp. 2478-2486 ◽  
Author(s):  
Andrea Giacometti ◽  
Oscar Cirioni ◽  
Roberto Ghiselli ◽  
Federico Mocchegiani ◽  
Fiorenza Orlando ◽  
...  
Keyword(s):  
Septic Shock ◽  
Antimicrobial Peptide ◽  
Gram Negative Bacteria ◽  
Amphibian Skin ◽  
Necrosis Factor Alpha ◽  
Gram Negative ◽  
Rat Models ◽  
E Coli ◽  
Tnf Α

ABSTRACT Sepsis remains a major cause of morbidity and mortality in hospitalized patients, despite intense efforts to improve survival. The primary lead for septic shock results from activation of host effector cells by endotoxin, the lipopolysaccharide (LPS) associated with cell membranes of gram-negative bacteria. For these reasons, the quest for compounds with antiendotoxin properties is actively pursued. We investigated the efficacy of the amphibian skin antimicrobial peptide temporin L in binding Escherichia coli LPS in vitro and counteracting its effects in vivo. Temporin L strongly bound to purified E. coli LPS and lipid A in vitro, as proven by fluorescent displacement assay, and readily penetrated into E. coli LPS monolayers. Furthermore, the killing activity of temporin L against E. coli was progressively inhibited by increasing concentrations of LPS added to the medium, further confirming the peptide's affinity for endotoxin. Antimicrobial assays showed that temporin L interacted synergistically with the clinically used β-lactam antibiotics piperacillin and imipenem. Therefore, we characterized the activity of temporin L when combined with imipenem and piperacillin in the prevention of lethality in two rat models of septic shock, measuring bacterial growth in blood and intra-abdominal fluid, endotoxin and tumor necrosis factor alpha (TNF-α) concentrations in plasma, and lethality. With respect to controls and single-drug treatments, the simultaneous administration of temporin L and β-lactams produced the highest antimicrobial activities and the strongest reduction in plasma endotoxin and TNF-α levels, resulting in the highest survival rates.

scholarly journals Improved Derivatives of Bactenecin, a Cyclic Dodecameric Antimicrobial Cationic Peptide

1999 ◽  
Vol 43 (5) ◽  
pp. 1274-1276 ◽  
Author(s):  
Manhong Wu ◽  
Robert E. W. Hancock
Keyword(s):  
Amino Acid ◽  
Antimicrobial Peptide ◽  
Tryptophan Residue ◽  
Gram Negative Bacteria ◽  
Cationic Peptide ◽  
Gram Positive ◽  
Antimicrobial Spectrum ◽  
Gram Negative ◽  
Derivatives Of

ABSTRACT Both linear and cyclic derivatives of the cyclic 12-amino-acid antimicrobial peptide bactenecin were designed based on optimization of amphipathicity and charge location. In general, increasing the number of positive charges at the N and C termini and adding an extra tryptophan residue in the loop not only increased the activities against both gram-positive and gram-negative bacteria but also broadened the antimicrobial spectrum.

scholarly journals Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria

1997 ◽  
Vol 1327 (1) ◽  
pp. 119-130 ◽  
Author(s):  
Katsumi Matsuzaki ◽  
Ken-ichi Sugishita ◽  
Mitsunori Harada ◽  
Nobutaka Fujii ◽  
Koichiro Miyajima
Keyword(s):  
Antimicrobial Peptide ◽  
Gram Negative Bacteria ◽  
Gram Negative

scholarly journals “Clicking” an Ionic Liquid to a Potent Antimicrobial Peptide: On the Route towards Improved Stability

2020 ◽  
Vol 21 (17) ◽  
pp. 6174
Author(s):  
Ana Gomes ◽  
Lucinda J. Bessa ◽  
Patrícia Correia ◽  
Iva Fernandes ◽  
Ricardo Ferraz ◽  
...  
Keyword(s):  
Ionic Liquid ◽  
Ionic Liquids ◽  
Klebsiella Pneumoniae ◽  
Antimicrobial Peptide ◽  
Clinical Isolate ◽  
Bioactive Peptides ◽  
Multidrug Resistant ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Improved Stability

A covalent conjugate between an antibacterial ionic liquid and an antimicrobial peptide was produced via “click” chemistry, and found to retain the parent peptide’s activity against multidrug-resistant clinical isolates of Gram-negative bacteria, and antibiofilm action on a resistant clinical isolate of Klebsiella pneumoniae, while exhibiting much improved stability towards tyrosinase-mediated modifications. This unprecedented communication is a prelude for the promise held by ionic liquids -based approaches as tools to improve the action of bioactive peptides.

scholarly journals Construction of p16Slux, a Novel Vector for Improved Bioluminescent Labeling of Gram-Negative Bacteria

2007 ◽  
Vol 73 (21) ◽  
pp. 7092-7095 ◽  
Author(s):  
Christian U. Riedel ◽  
Pat G. Casey ◽  
Heidi Mulcahy ◽  
Fergal O'Gara ◽  
Cormac G. M. Gahan ◽  
...  
Keyword(s):  
Bacterial Chromosome ◽  
Gram Negative Bacteria ◽  
Site Specific ◽  
Gram Negative ◽  
Site Specific Integration ◽  
Murine Infections

ABSTRACT A novel vector has been constructed for the constitutive luminescent tagging of gram-negative bacteria by site-specific integration into the 16S locus of the bacterial chromosome. A number of gram-negative pathogens were successfully tagged using this vector, and the system was validated during murine infections of living animals.

scholarly journals Formation of a β-barrel membrane protein is catalyzed by the interior surface of the assembly machine protein BamA

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
James Lee ◽  
David Tomasek ◽  
Thiago MA Santos ◽  
Mary D May ◽  
Ina Meuskens ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Molecular Mechanisms ◽  
Gram Negative Bacteria ◽  
Site Specific ◽  
Gram Negative ◽  
Interior Surface ◽  
Essential Component ◽  
Bam Complex ◽  
Β Sheet

The β-barrel assembly machine (Bam) complex in Gram-negative bacteria and its counterparts in mitochondria and chloroplasts fold and insert outer membrane β-barrel proteins. BamA, an essential component of the complex, is itself a β-barrel and is proposed to play a central role in assembling other barrel substrates. Here, we map the path of substrate insertion by the Bam complex using site-specific crosslinking to understand the molecular mechanisms that control β-barrel folding and release. We find that the C-terminal strand of the substrate is stably held by BamA and that the N-terminal strands of the substrate are assembled inside the BamA β-barrel. Importantly, we identify contacts between the assembling β-sheet and the BamA interior surface that determine the rate of substrate folding. Our results support a model in which the interior wall of BamA acts as a chaperone to catalyze β-barrel assembly.

scholarly journals NMR Study of the Secondary Structure and Biopharmaceutical Formulation of an Active Branched Antimicrobial Peptide

Molecules ◽  
2019 ◽  
Vol 24 (23) ◽  
pp. 4290 ◽  
Author(s):  
Francesca Castiglia ◽  
Fabrizia Zevolini ◽  
Giulia Riolo ◽  
Jlenia Brunetti ◽  
Alessandra De Lazzari ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Antimicrobial Peptide ◽  
Process Development ◽  
Pharmacokinetic Profile ◽  
Point Of View ◽  
Resistant Bacteria ◽  
Gram Negative Bacteria ◽  
Acinetobacter Baumanii ◽  
Gram Negative ◽  
Nmr Study

The synthetic antimicrobial peptide SET-M33 is being developed as a possible new antibacterial candidate for the treatment of multi-drug resistant bacteria. SET-M33 is a branched peptide featuring higher resistance and bioavailability than its linear analogues. SET-M33 shows antimicrobial activity against different species of multi-resistant Gram-negative bacteria, including clinically isolated strains of Pseudomonas aeruginosa, Klebsiella pneumoniae, Acinetobacter baumanii and Escherichia coli. The secondary structure of this 40 amino acid peptide was investigated by NMR to fully characterize the product in the framework of preclinical studies. The possible presence of helixes or β-sheets in the structure had to be explored to predict the behavior of the branched peptide in solution, with a view to designing a formulation for parenteral administration. Since the final formulation of SET-M33 will be strictly defined in terms of counter-ions and additives, we also report the studies on a new salt form, SET-M33 chloride, that retains its activity against Gram-negative bacteria and gains in solubility, with a possible improvement in the pharmacokinetic profile. The opportunity of using a chloride counter-ion is very convenient from a process development point of view and did not increase the toxicity of the antimicrobial drug.

Inhibition of Food-Borne Pathogens by T1, a Novel Antimicrobial Peptide as a Potential Food Preservative

2008 ◽  
Vol 4 (4) ◽  
Author(s):  
Yali Tang ◽  
Yonghui Shi ◽  
Wei Zhao ◽  
Gang Hao ◽  
Guowei Le
Keyword(s):  
Antimicrobial Peptide ◽  
Gram Negative Bacteria ◽  
Food Preservative ◽  
Recombinant Peptide ◽  
Gram Negative ◽  
Food Borne Pathogens ◽  
Theoretical Design ◽  
Food Borne ◽  
Antimicrobial Mechanism ◽  
Potential Food

An efficient and convenient purifying procedure for recombinant peptide was established. Thereby, the aimed antimicrobial peptide T1 containing the conservative sequences derived from cecropin was successfully expressed and purified. The composition of amino acid of the purified peptide T1 was consistent with that of theoretical design. The significant antimicrobial activity of T1 against gram-positive and gram-negative bacteria was demonstrated, suggesting that the conservative sequences in cecropin play an important role in the antimicrobial mechanism and that antimicrobial peptide T1 has the potential to be used as the food preservative.

Combating multidrug-resistant Gram-negative bacteria with structurally nanoengineered antimicrobial peptide polymers

2016 ◽  
Vol 1 (11) ◽  
Author(s):  
Shu J. Lam ◽  
Neil M. O'Brien-Simpson ◽  
Namfon Pantarat ◽  
Adrian Sulistio ◽  
Edgar H. H. Wong ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Multidrug Resistant ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Peptide Polymers
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