Interaction of the cationic peptide bactenecin with mixed phospholipid monolayers at the air–water interface

López‐Oyama, A.B.; Taboada, Pablo; Burboa, María G.; Rodríguez, Ezequiel; Mosquera, Vı́ctor; Váldez, Miguel A.

doi:10.1016/j.jcis.2011.03.081

Cited by 16 publications

(15 citation statements)

References 84 publications

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“…Therefore, The β-hairpin model was generated using a “non-canonical” β-hairpin template of cystatin (PDB file 1cew, fragment 50–61), which allows the arrangement of Cys 3 and Cys 11 residues in such a way as to form the disulfide across the non-hydrogen bonded pair of residues and the formation of a 3-residue β-turn in α R γ R β conformation. In this bactenecin model, the disulfide bridge has the gauche-gauche-gauche conformation, in agreement with experimental data [45]. After substituting all the residues in the template using QUANTA (Accelrys Software Inc.) and minimization of local energy by CHARMM (200 steps with adopted basis Newton-Raphson method, ε = 10), the models were positioned in the lipid bilayer using our program PPM 2.0 [38].…”

Section: Methodssupporting

confidence: 80%

“…Recent experimental studies indicated that Arg-rich bactenecin has a β-turn structure stabilized by a disulfide bridge in a distinct conformation that does not change significantly upon incorporation of the peptide into the lipid monolayer [45]. In addition, it has been observed that bactenecin is prone to self-association and formation of filament-like structures on membrane surfaces [45].…”

Section: Resultsmentioning

confidence: 99%

“…In addition, it has been observed that bactenecin is prone to self-association and formation of filament-like structures on membrane surfaces [45]. Therefore, we modeled the structure of bactenecin as a β-hairpin capable of self assembling into a larger β-sheet.…”

Section: Resultsmentioning

confidence: 99%

“…Intensive study on this short cationic peptide to modify its selectivity and activity expanded from engineering bactenecin to be in a looped or linear form to performing amino acid substitutions in order to increase or decrease the peptide hydrophobicity [15]–[17]. Recent reports also show that the oligomeric status of bactenecin determines its mode of action and dictates the strength of the antimicrobial activity [18]–[20].…”

Section: Introductionmentioning

confidence: 99%

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Antimicrobial Action of the Cyclic Peptide Bactenecin on Burkholderia pseudomallei Correlates with Efficient Membrane Permeabilization

et al. 2013

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Burkholderia pseudomallei is a category B agent that causes Melioidosis, an acute and chronic disease with septicemia. The current treatment regimen is a heavy dose of antibiotics such as ceftazidime (CAZ); however, the risk of a relapse is possible. Peptide antibiotics are an alternative to classical antibiotics as they exhibit rapid action and are less likely to result in the development of resistance. The aim of this study was to determine the bactericidal activity against B. pseudomallei and examine the membrane disrupting abilities of the potent antimicrobial peptides: bactenecin, RTA3, BMAP-18 and CA-MA. All peptides exhibited >97% bactericidal activity at 20 µM, with bactenecin having slightly higher activity. Long term time-kill assays revealed a complete inhibition of cell growth at 50 µM bactenecin and CA-MA. All peptides inhibited biofilm formation comparable to CAZ, but exhibited faster kinetics (within 1 h). Bactenecin exhibited stronger binding to LPS and induced perturbation of the inner membrane of live cells. Interaction of bactenecin with model membranes resulted in changes in membrane fluidity and permeability, leading to leakage of dye across the membrane at levels two-fold greater than that of other peptides. Modeling of peptide binding on the membrane showed stable and deep insertion of bactenecin into the membrane (up to 9 Å). We propose that bactenecin is able to form dimers or large β-sheet structures in a concentration dependent manner and subsequently rapidly permeabilize the membrane, leading to cytosolic leakage and cell death in a shorter period of time compared to CAZ. Bactenecin might be considered as a potent antimicrobial agent for use against B. pseudomallei.

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Section: Methodssupporting

confidence: 80%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Antimicrobial Action of the Cyclic Peptide Bactenecin on Burkholderia pseudomallei Correlates with Efficient Membrane Permeabilization

et al. 2013

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“…Upon increasing peptide concentration from 16 to 90 mg mL -1 , planar-like carpet domains were created [34,35].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Interactions of bioactive molecules & nanomaterials with Langmuir monolayers as cell membrane models

et al. 2015

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One‐Pot Synthesis of a Cyclic Antimicrobial Peptide‐Conjugated Phthalocyanine for Synergistic Chemo‐Photodynamic Killing of Multidrug‐Resistant Bacteria

Chu

Chin

Wong

et al. 2020

Advanced Therapeutics

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Multidrug-resistant (MDR) bacteria pose a serious threat to public health globally. Among the various antimicrobial modalities that have recently emerged, photodynamic therapy has received considerable attention because of its various potential advantages, including the unlikelihood of inducing drug resistance. A facile synthetic approach is reported to prepare a phthalocyanine-based photosensitizer conjugated with a cyclic bactenecin peptide. This one-pot procedure that involves site-selective alkylation of the two cysteine residues of a linear bactenecin peptide followed by Diels-Alder reaction leads to the formation of the conjugate labeled as cBac-Pc in 27% isolated yield. As shown by confocal fluorescence microscopy, this conjugate shows selective affinity toward bacterial over mammalian cells. It can also induce synergistic cytotoxic effects due to the cyclic peptide and phthalocyanine against a spectrum of Gram-positive and Gram-negative bacterial strains, including two ATCC-type strains and two clinical isolates of MDR bacterial strains. It is believed that the inhibition mechanism is based on the physical destruction of the cell membrane due to the cyclic peptide followed by photodynamic action induced by the phthalocyanine unit. Multidrug-resistant (MDR) bacteria have become a serious threat to public health that is accounting for at least 700 000 deaths

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Interaction of the cationic peptide bactenecin with mixed phospholipid monolayers at the air–water interface

Cited by 16 publications

References 84 publications

Antimicrobial Action of the Cyclic Peptide Bactenecin on Burkholderia pseudomallei Correlates with Efficient Membrane Permeabilization

Antimicrobial Action of the Cyclic Peptide Bactenecin on Burkholderia pseudomallei Correlates with Efficient Membrane Permeabilization

Interactions of bioactive molecules & nanomaterials with Langmuir monolayers as cell membrane models

One‐Pot Synthesis of a Cyclic Antimicrobial Peptide‐Conjugated Phthalocyanine for Synergistic Chemo‐Photodynamic Killing of Multidrug‐Resistant Bacteria

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