“Doubly Selective” Antimicrobial Polymers: How Do They Differentiate between Bacteria?

Lienkamp, Karen; Kumar, Kushi-Nidhi; Som, Abhigyan; Nüsslein, Klaus; Tew, Gregory N.

doi:10.1002/chem.200802558

Cited by 154 publications

(181 citation statements)

References 22 publications

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“…Thus, the higher MIC values in the case of S. aureus compared to E. coli might result from a sieving effect by the thick peptidoglycan layer of the Gram-positive bacterium. This was also discussed by Lienkamp et al [43].…”

Section: Antibacterial Efficacysupporting

confidence: 64%

Novel Antibacterial Polyglycidols: Relationship between Structure and Properties

et al. 2018

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Antimicrobial polymers are an attractive alternative to low molecular weight biocides, because they are non-volatile, chemically stable, and can be used as non-releasing additives. Polymers with pendant quaternary ammonium groups and hydrophobic chains exhibit antimicrobial properties due to the electrostatic interaction between polymer and cell wall, and the membrane disruptive capabilities of the hydrophobic moiety. Herein, the synthesis of cationic-hydrophobic polyglycidols with varying structures by post-polymerization modification is presented. The antimicrobial properties of the prepared polyglycidols against E. coli and S. aureus are examined. Polyglycidol with statistically distributed cationic and hydrophobic groups (cationic-hydrophobic balance of 1:1) is compared to (i) polyglycidol with a hydrophilic modification at the cationic functionality; (ii) polyglycidol with both-cationic and hydrophobic groups-at every repeating unit; and (iii) polyglycidol with a cationic-hydrophobic balance of 1:2. A relationship between structure and properties is presented.

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Section: Antibacterial Efficacysupporting

confidence: 64%

Novel Antibacterial Polyglycidols: Relationship between Structure and Properties

et al. 2018

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“…Gram-negative bacteria (such as E. coli) have an outer membrane and a plasma membrane with a thin layer of peptidoglycan between them, and thick layer of lipopolysaccharide on the outer membrane surface (Lienkamp et al 2009). Although AFM allows us to obtain images and track the changes of the intact bacterial surface in very good resolution, it is not enough to interpret the measurements, considering the complexity of mechanism of action of AMPs.…”

Section: Discussionmentioning

confidence: 99%

Interaction of cysteine-rich cationic antimicrobial peptides with intact bacteria and model membranes

Nagy

Mikuláss

Végh

et al. 2015

gpb

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Abstract. Antimicrobial peptides are small proteins that exhibit a broad spectrum of antimicrobial activity. Their chemical structure allows them to interact (attach and insert) with membranes. The fine details about this interaction and their mode of action are not fully clarified yet. In order to better understand this mechanism, we have performed in situ atomic force microscopy studies using two types of nodule specific cysteine-rich NCR peptides on Escherichia coli bacteria and on natural purple membrane. On intact bacteria, both NCR247 and NCR335 caused increase in the surface roughness, indicating the damage of the bacterial cell envelope. In case of the tightly packed purple membrane, it is clear that the peptides prefer to disrupt the border of the disks indicating a strong lipid preference of the interaction. These results verify the concept that the first target of NCR peptides is probably the bacterial cell envelope, especially the lipid matrix.

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“…The P 0 and other PMAs with low MP methyl tend to be more selective to S. aureus and B. subtilis over other bacteria tested. Lienkamp et al previously reported that cationic polynorbornenes showed significantly higher activity against S. aureus compared to E. coli [47,48]. The authors demonstrated that the double membrane structure of E. coil cell wall likely limits the access of the polymers to the cytoplasmic membrane [48].…”

Section: Activity Spectrummentioning

confidence: 97%

“…Lienkamp et al previously reported that cationic polynorbornenes showed significantly higher activity against S. aureus compared to E. coli [47,48]. The authors demonstrated that the double membrane structure of E. coil cell wall likely limits the access of the polymers to the cytoplasmic membrane [48]. Epand et al reported that an acyl-Lys oligomer is bacteriostatic, and it does not compromise the cell membrane of S. aureus [49].…”

Section: Activity Spectrummentioning

confidence: 99%

Activity and Mechanism of Antimicrobial Peptide-Mimetic Amphiphilic Polymethacrylate Derivatives

et al. 2011

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Cationic amphiphilic polymethacrylate derivatives (PMAs) have shown potential as a novel class of synthetic antimicrobials. A panel of PMAs with varied ratios of hydrophobic and cationic side chains were synthesized and tested for antimicrobial activity and mechanism of action. The PMAs are shown to be active against a panel of pathogenic bacteria, including a drug-resistant Staphylococcus aureus, compared to the natural antimicrobial peptide magainin which did not display any activity against the same strain. The selected PMAs with 47-63% of methyl groups in the side chains showed minimum inhibitory concentrations of ≤2-31 µg/mL, but cause only minimal harm to human red blood cells. The PMAs also exhibit rapid bactericidal kinetics. Culturing Escherichia coli in the presence of the PMAs did not exhibit any potential to develop resistance against the PMAs. The antibacterial activities of PMAs against E. coli and S. aureus were slightly reduced in the presence of physiological salts. The activity of PMAs showed bactericidal effects against E. coli and S. aureus in both exponential and stationary growth phases. These results demonstrate that PMAs are a new antimicrobial platform with no observed development of resistance in bacteria. In addition, the PMAs permeabilized the E. coli outer membrane at polymer concentrations lower than their MIC values, but they did not show any effect on the bacterial inner membrane. This indicates that mechanisms other than membrane permeabilization may be the primary factors determining their antimicrobial activity.

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“Doubly Selective” Antimicrobial Polymers: How Do They Differentiate between Bacteria?

Cited by 154 publications

References 22 publications

Novel Antibacterial Polyglycidols: Relationship between Structure and Properties

Novel Antibacterial Polyglycidols: Relationship between Structure and Properties

Interaction of cysteine-rich cationic antimicrobial peptides with intact bacteria and model membranes

Activity and Mechanism of Antimicrobial Peptide-Mimetic Amphiphilic Polymethacrylate Derivatives

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