scholarly journals Localization of antimicrobial peptides on polymerized liposomes leading to their enhanced efficacy against Pseudomonas aeruginosa

2011 ◽  
Vol 7 (3) ◽  
pp. 711 ◽  
Author(s):  
Amit Kumar ◽  
Satya S. Kolar ◽  
Meriong Zao ◽  
Alison M. McDermott ◽  
Chengzhi Cai
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Antimicrobial Peptides ◽  
Polymerized Liposomes

scholarly journals Mechanism of Action of Surface Immobilized Antimicrobial Peptides Against Pseudomonas aeruginosa

2020 ◽  
Vol 10 ◽  
Author(s):  
Muhammad Yasir ◽  
Debarun Dutta ◽  
Khondker R. Hossain ◽  
Renxun Chen ◽  
Kitty K. K. Ho ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Antimicrobial Peptides ◽  
Mechanism Of Action

scholarly journals Synthetic Antimicrobial Peptides Exhibit Two Different Binding Mechanisms to the Lipopolysaccharides Isolated from Pseudomonas aeruginosa and Klebsiella pneumoniae

2014 ◽  
Vol 2014 ◽  
pp. 1-13 ◽  
Author(s):  
Hanbo Chai ◽  
William E. Allen ◽  
Rickey P. Hicks
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Klebsiella Pneumoniae ◽  
Antimicrobial Peptides ◽  
Inhibitory Activity ◽  
Binding Conformation ◽  
Cd Studies ◽  
Synthetic Antimicrobial Peptides ◽  
Activity Mechanism ◽  
Binding Mechanisms

Circular dichroism and 1H NMR were used to investigate the interactions of a series of synthetic antimicrobial peptides (AMPs) with lipopolysaccharides (LPS) isolated from Pseudomonas aeruginosa and Klebsiella pneumoniae. Previous CD studies with AMPs containing only three Tic-Oic dipeptide units do not exhibit helical characteristics upon interacting with small unilamellar vesicles (SUVs) consisting of LPS. Increasing the number of Tic-Oic dipeptide units to six resulted in five analogues with CD spectra that exhibited helical characteristics on binding to LPS SUVs. Spectroscopic and in vitro inhibitory data suggest that there are two possible helical conformations resulting from two different AMP-LPS binding mechanisms. Mechanism one involves a helical binding conformation where the AMP binds LPS very strongly and is not efficiently transported across the LPS bilayer resulting in the loss of inhibitory activity. Mechanism two involves a helical binding conformation where the AMP binds LPS very loosely and is efficiently transported across the LPS bilayer resulting in an increase in inhibitory activity. Mechanism three involves a nonhelical binding conformation where the AMP binds LPS very loosely and is efficiently transported across the LPS bilayer resulting in an increase in inhibitory activity.

scholarly journals PmrAB, a Two-Component Regulatory System of Pseudomonas aeruginosa That Modulates Resistance to Cationic Antimicrobial Peptides and Addition of Aminoarabinose to Lipid A

2004 ◽  
Vol 186 (2) ◽  
pp. 575-579 ◽  
Author(s):  
Samuel M. Moskowitz ◽  
Robert K. Ernst ◽  
Samuel I. Miller
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Antimicrobial Peptides ◽  
Lipid A ◽  
Regulatory System ◽  
Signal Transduction System ◽  
Cationic Antimicrobial Peptides ◽  
Two Component ◽  
Serovar Typhimurium ◽  
Two Component Signal Transduction ◽  
Resistant Mutants

ABSTRACT Spontaneous polymyxin-resistant mutants of Pseudomonas aeruginosa were isolated. The mutations responsible for this phenotype were mapped to a two-component signal transduction system similar to PmrAB of Salmonella enterica serovar Typhimurium. Lipid A of these mutants contained aminoarabinose, an inducible modification that is associated with polymyxin resistance. Thus, P. aeruginosa possesses a mechanism that induces resistance to cationic antimicrobial peptides in response to environmental conditions.

scholarly journals Production and Purification of Two Bioactive Antimicrobial Peptides Using a Two-Step Approach Involving an Elastin-Like Fusion Tag

2021 ◽  
Vol 14 (10) ◽  
pp. 956
Author(s):  
Ana Margarida Pereira ◽  
André da Costa ◽  
Simoni Campos Dias ◽  
Margarida Casal ◽  
Raul Machado
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Klebsiella Pneumoniae ◽  
Antimicrobial Peptides ◽  
Formic Acid ◽  
Cleavage Site ◽  
Burkholderia Cenocepacia ◽  
High Recovery ◽  
Temperature Cycles ◽  
Acid Cleavage

Antimicrobial resistance is an increasing global threat, demanding new therapeutic biomolecules against multidrug-resistant bacteria. Antimicrobial peptides (AMPs) are promising candidates for a new generation of antibiotics, but their potential application is still in its infancy, mostly due to limitations associated with large-scale production. The use of recombinant DNA technology for the production of AMPs fused with polymer tags presents the advantage of high-yield production and cost-efficient purification processes at high recovery rates. Owing to their unique properties, we explored the use of an elastin-like recombinamer (ELR) as a fusion partner for the production and isolation of two different AMPs (ABP-CM4 and Synoeca-MP), with an interspacing formic acid cleavage site. Recombinant AMP-ELR proteins were overproduced in Escherichia coli and efficiently purified by temperature cycles. The introduction of a formic acid cleavage site allowed the isolation of AMPs, resorting to a two-step methodology involving temperature cycles and a simple size-exclusion purification step. This simple and easy-to-implement purification method was demonstrated to result in high recovery rates of bioactive AMPs. The minimum inhibitory concentration (MIC) of the free AMPs was determined against seven different bacteria of clinical relevance (Staphylococcus aureus, Staphylococcus epidermidis, Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa, and two Burkholderia cenocepacia strains), in accordance with the EUCAST/CLSI antimicrobial susceptibility testing standards. All the bacterial strains (except for Pseudomonas aeruginosa) were demonstrated to be susceptible to ABP-CM4, including a resistant Burkholderia cenocepacia clinical strain. As for Synoeca-MP, although it did not inhibit the growth of Pseudomonas aeruginosa or Klebsiella pneumoniae, it was demonstrated to be highly active against the remaining bacteria. The present work provides the basis for the development of an efficient and up-scalable biotechnological platform for the production and purification of active AMPs against clinically relevant bacteria.

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