scholarly journals Insights into the Action Mechanism of the Antimicrobial Peptide Lasioglossin III

2021 ◽  
Vol 22 (6) ◽  
pp. 2857
Author(s):  
Filomena Battista ◽  
Rosario Oliva ◽  
Pompea Del Vecchio ◽  
Roland Winter ◽  
Luigi Petraccone
Keyword(s):  
Antimicrobial Peptide ◽  
Gram Negative Bacteria ◽  
Lipid Domains ◽  
Action Mechanism ◽  
Cationic Antimicrobial Peptide ◽  
Intracellular Targeting ◽  
Gel Retardation Assay ◽  
Charged Membrane ◽  
Intracellular Target ◽  
Anionic Lipids

Lasioglossin III (LL-III) is a cationic antimicrobial peptide derived from the venom of the eusocial bee Lasioglossum laticeps. LL-III is extremely toxic to both Gram-positive and Gram-negative bacteria, and it exhibits antifungal as well as antitumor activity. Moreover, it shows low hemolytic activity, and it has almost no toxic effects on eukaryotic cells. However, the molecular basis of the LL-III mechanism of action is still unclear. In this study, we characterized by means of calorimetric (DSC) and spectroscopic (CD, fluorescence) techniques its interaction with liposomes composed of a mixture of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1-palmitoyl-2-oleoyl-sn-glycero-3-rac-phosphoglycerol (POPG) lipids as a model of the negatively charged membrane of pathogens. For comparison, the interaction of LL-III with the uncharged POPC liposomes was also studied. Our data showed that LL-III preferentially interacted with anionic lipids in the POPC/POPG liposomes and induces the formation of lipid domains. Furthermore, the leakage experiments showed that the peptide could permeabilize the membrane. Interestingly, our DSC results showed that the peptide-membrane interaction occurs in a non-disruptive manner, indicating an intracellular targeting mode of action for this peptide. Consistent with this hypothesis, our gel-retardation assay experiments showed that LL-III could interact with plasmid DNA, suggesting a possible intracellular target.

scholarly journals Antimicrobial Peptide Novicidin Synergizes with Rifampin, Ceftriaxone, and Ceftazidime against Antibiotic-Resistant EnterobacteriaceaeIn Vitro

2015 ◽  
Vol 59 (10) ◽  
pp. 6233-6240 ◽  
Author(s):  
Odel Soren ◽  
Karoline Sidelmann Brinch ◽  
Dipesh Patel ◽  
Yingjun Liu ◽  
Alexander Liu ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Bacterial Infections ◽  
New Drugs ◽  
Gram Negative Bacteria ◽  
Cationic Antimicrobial Peptide ◽  
Antibiotic Resistant ◽  
Gram Negative ◽  
Resistant Strains ◽  
Multiple Strains

ABSTRACTThe spread of antibiotic resistance among Gram-negative bacteria is a serious clinical threat, and infections with these organisms are a leading cause of mortality worldwide. Traditional novel drug development inevitably leads to the emergence of new resistant strains, rendering the new drugs ineffective. Therefore, reviving the therapeutic potentials of existing antibiotics represents an attractive novel strategy. Novicidin, a novel cationic antimicrobial peptide, is effective against Gram-negative bacteria. Here, we investigated novicidin as a possible antibiotic enhancer. The actions of novicidin in combination with rifampin, ceftriaxone, or ceftazidime were investigated against 94 antibiotic-resistant clinical Gram-negative isolates and 7 strains expressing New Delhi metallo-β-lactamase-1. Using the checkerboard method, novicidin combined with rifampin showed synergy with >70% of the strains, reducing the MICs significantly. The combination of novicidin with ceftriaxone or ceftazidime was synergistic against 89.7% of the ceftriaxone-resistant strains and 94.1% of the ceftazidime-resistant strains. Synergistic interactions were confirmed using time-kill studies with multiple strains. Furthermore, novicidin increased the postantibiotic effect when combined with rifampin or ceftriaxone. Membrane depolarization assays revealed that novicidin alters the cytoplasmic membrane potential of Gram-negative bacteria.In vitrotoxicology tests showed novicidin to have low hemolytic activity and no detrimental effect on cell cultures. We demonstrated that novicidin strongly rejuvenates the therapeutic potencies of ceftriaxone or ceftazidime against resistant Gram-negative bacteriain vitro. In addition, novicidin boosted the activity of rifampin. This strategy can have major clinical implications in our fight against antibiotic-resistant bacterial infections.

Highly efficient nanomedicine from cationic antimicrobial peptide-protected Ag nanoclusters

2021 ◽  
Author(s):  
Zhikai Ye ◽  
Haishuang Zhu ◽  
Shan Zhang ◽  
Jing Li ◽  
Jin Wang ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Biological Systems ◽  
Cationic Antimicrobial Peptide ◽  
Highly Efficient ◽  
Antimicrobial Efficiency ◽  
Ag Nanoclusters ◽  
Fine Tune

Designing the homogeneous assembly of the bio–nano interface to fine-tune the interactions between the nanoprobes and biological systems is of prime importance to improve the antimicrobial efficiency of nanomedicines.

scholarly journals Encapsulation of a cationic antimicrobial peptide into self-assembled polyion complex nano-objects enhances its antitumor properties

2022 ◽  
Vol 1249 ◽  
pp. 131482
Author(s):  
Mina Răileanu ◽  
Barbara Lonetti ◽  
Charles-Louis Serpentini ◽  
Dominique Goudounèche ◽  
Laure Gibot ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Cationic Antimicrobial Peptide ◽  
Polyion Complex ◽  
Antitumor Properties ◽  
Self Assembled

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.

Spermicidal efficacy of VRP, a synthetic cationic antimicrobial peptide, inducing apoptosis and membrane disruption

2017 ◽  
Vol 233 (2) ◽  
pp. 1041-1050 ◽  
Author(s):  
Prasanta Ghosh ◽  
Arpita Bhoumik ◽  
Sudipta Saha ◽  
Sandipan Mukherjee ◽  
Sarfuddin Azmi ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Membrane Disruption ◽  
Cationic Antimicrobial Peptide

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.

Sign in / Sign up

Export Citation Format

Share Document