Efficacy of six frog skin-derived antimicrobial peptides against colistin-resistant strains of the Acinetobacter baumannii group

Conlon, J. Michael; Sonnevend, Ágnes; Pál, Tibor; Vila-Farrés, Xavier

doi:10.1016/j.ijantimicag.2011.12.005

Cited by 26 publications

(22 citation statements)

References 29 publications

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“…At least one of these mechanisms causes very high resistance to colistin but does not appear to impact, to the same extent, susceptibility to AMPs and ceragenins. These observations are consistent with the reported susceptibility of colistin-resistant bacteria to a variety of AMPs (36, 37). The fact that lead ceragenins (CSA-44 and CSA-131) retain bactericidal activity against highly colistin-resistant bacteria provides further support for development of these compounds as broad-spectrum antibacterial agents in multiple potential clinical applications.…”

Section: Textsupporting

confidence: 92%

Susceptibility of Colistin-Resistant, Gram-Negative Bacteria to Antimicrobial Peptides and Ceragenins

Hashemi

Rovig

Weber

et al. 2017

Antimicrob Agents Chemother

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The susceptibility of colistin-resistant clinical isolates of Klebsiella pneumoniae to ceragenins and antimicrobial peptides (AMPs) suggests that there is little to no cross-resistance between colistin and ceragenins/AMPs and that lipid A modifications are found in bacteria with modest changes in susceptibility to ceragenins and with high levels of resistance to colistin. These results suggest that there are differences in the resistance mechanisms to colistin and ceragenins/AMPs.

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Section: Textsupporting

confidence: 92%

Susceptibility of Colistin-Resistant, Gram-Negative Bacteria to Antimicrobial Peptides and Ceragenins

Hashemi

Rovig

Weber

et al. 2017

Antimicrob Agents Chemother

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“…They also tested the in vivo activity with this peptide and only observed a local effect due to low in vivo stability [23]. Another peptide that has been described is api88 (Gu-ONNRP-VYIPRPRPPHPRL-NH 2 ) [24], which was found to be active against the most common Gram-negative pathogens such as E. coli, P. aeruginosa, K. pneumoniae or A. baumannii with MIC values Nonetheless, the cytoxicity and stability of these peptides were not optimized, and therefore, their activity in vivo may actually be very low [25]. Leakage assays were performed using two different membrane mimetics, a negatively charged membrane mimicking bacterial membranes, and a neutral membrane.…”

Section: Mastoparan Analogues Rational Design and Synthesis Activitmentioning

confidence: 99%

“…Taking this scenario into account, there is an urgent need for new options to fight against this pathogen. One possible option is the use of antimicrobial peptides (AMPs) [9e11], and especially peptides isolated from a natural source [12]. One of the main drawbacks of using peptides as antimicrobial agents is the low stability or half-life in human serum due to the action of peptidases and proteases present in the human body [13], however there are several ways to increase their stability, such as using fluorinated peptides [14,15].…”

Section: Introductionmentioning

confidence: 99%

Sequence-activity relationship, and mechanism of action of mastoparan analogues against extended-drug resistant Acinetobacter baumannii

Vila-Farrés

López-Rojas

Pachón-Ibáñez

et al. 2015

European Journal of Medicinal Chemistry

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The treatment of some infectious diseases can currently be very challenging since the spread of multi-, extended- or pan-resistant bacteria has considerably increased over time. On the other hand, the number of new antibiotics approved by the FDA has decreased drastically over the last 30 years. The main objective of this study was to investigate the activity of wasp peptides, specifically mastoparan and some of its derivatives against extended-resistant Acinetobacter baumannii. We optimized the stability of mastoparan in human serum since the specie obtained after the action of the enzymes present in human serum is not active. Thus, 10 derivatives of mastoparan were synthetized. Mastoparan analogues (guanidilated at the N-terminal, enantiomeric version and mastoparan with an extra positive charge at the C-terminal) showed the same activity against Acinetobacter baumannii as the original peptide (2.7 μM) and maintained their stability to more than 24 h in the presence of human serum compared to the original compound. The mechanism of action of all the peptides was carried out using a leakage assay. It was shown that mastoparan and the abovementioned analogues were those that released more carboxyfluorescein. In addition, the effect of mastoparan and its enantiomer against A. baumannii was studied using transmission electron microscopy (TEM). These results suggested that several analogues of mastoparan could be good candidates in the battle against highly resistant A. baumannii infections since they showed good activity and high stability.

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“…In another study [133], six cationic a-helical frog skin-derived peptides (CPF-AM1, PGLa-AM1, B2RP-ERa, [E4K]alyteserin-1c, [D4K]B2RP and [G4K]XT-7) were selected for their potent growth-inhibitory activity against Gram-negative bacteria and low hemolytic activity against human erythrocytes. All these peptides were active against colistin-susceptible and colistin-resistant clinical MDR strains of A. baumannii and A. nosocomialis.…”

Section: Combination Of Antibacterial Agentsmentioning

confidence: 99%

Therapeutic options forAcinetobacter baumanniiinfections: an update

Vila

Pachón

2012

Expert Opinion on Pharmacotherapy

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With the increase in resistance to carbapenems, colistin has been extensively used, however some data suggest that the doses recommended are insufficient before a steady state is reached, suggesting that the administration of a loading dose on initiation of treatment may be beneficial. Combinations of antibacterial agents such as impenem plus sulbactam or imipenem plus colistin have been successfully used to treat VAP. Nonetheless, future alternatives for treating A. baumannii infections should be explored.

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Efficacy of six frog skin-derived antimicrobial peptides against colistin-resistant strains of the Acinetobacter baumannii group

Cited by 26 publications

References 29 publications

Susceptibility of Colistin-Resistant, Gram-Negative Bacteria to Antimicrobial Peptides and Ceragenins

Susceptibility of Colistin-Resistant, Gram-Negative Bacteria to Antimicrobial Peptides and Ceragenins

Sequence-activity relationship, and mechanism of action of mastoparan analogues against extended-drug resistant Acinetobacter baumannii

Therapeutic options forAcinetobacter baumanniiinfections: an update

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