Effect of SDS and CTAB on Derivatives of Antimicrobial Peptides Arenicin and LL-37

Dannehl, Claudia; Travkova, Oksana G.; Brezesinski, Gerald

doi:10.1246/cl.2012.1178

Cited by 3 publications

(3 citation statements)

References 21 publications

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“…On the other hand, it was the unique characteristic of P1 to maintain its original structure. AMPs (arenicin, LL-37, and RR12) adopted a predominant β-strand or random coil structure in an aqueous solution, but they underwent a conformational change with an increase in α-helix when complexed with SDS ( Dannehl, Travkova & Brezesinski, 2012 ; Krenev et al, 2020 ; Wu et al, 2020 ). In addition, some peptides (OM19R analogs) had the characteristics of random coil, and their structures did not significantly change in the presence of SDS, supporting that AMP-facilitated intracellular activities (increased DNA binding, reduced synthesis of intracellular proteins, and decreased intracellular ATP) influenced a microbial inhibition rather than membrane disintegration ( Zhao et al, 2021 ).…”

Section: Discussionmentioning

confidence: 99%

Anti-methicillin-resistant Staphylococcus aureus and antibiofilm activity of new peptides produced by a Brevibacillus strain

Ogunsile,

Songnaka,

Sawatdee

et al. 2023

PeerJ

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Background Methicillin-resistant Staphylococcus aureus (MRSA) is listed as a highly prioritized pathogen by the World Health Organization (WHO) to search for effective antimicrobial agents. Previously, we isolated a soil Brevibacillus sp. strain SPR19 from a botanical garden, which showed anti-MRSA activity. However, the active substances were still unknown. Methods The cell-free supernatant of this bacterium was subjected to salt precipitation, cation exchange, and reversed-phase chromatography. The antimicrobial activity of pure substances was determined by broth microdilution assay. The peptide sequences and secondary structures were characterized by tandem mass spectroscopy and circular dichroism (CD), respectively. The most active anti-MRSA peptide underwent a stability study, and its mechanism was determined through scanning electron microscopy, cell permeability assay, time-killing kinetics, and biofilm inhibition and eradication. Hemolysis was used to evaluate the peptide toxicity. Results The pure substances (BrSPR19-P1 to BrSPR19-P5) were identified as new peptides. Their minimum inhibition concentration (MIC) and minimum bactericidal concentration (MBC) against S. aureus and MRSA isolates ranged from 2.00 to 32.00 and 2.00 to 64.00 µg/mL, respectively. The sequence analysis of anti-MRSA peptides revealed a length ranging from 12 to 16 residues accompanied by an amphipathic structure. The physicochemical properties of peptides were predicted such as pI (4.25 to 10.18), net charge at pH 7.4 (−3 to +4), and hydrophobicity (0.12 to 0.96). The CD spectra revealed that all peptides in the water mainly contained random coil structures. The increased proportion of α-helix structure was observed in P2−P5 when incubated with SDS. P2 (NH2-MFLVVKVLKYVV-COOH) showed the highest antimicrobial activity and high stability under stressed conditions such as temperatures up to 100 °C, solution of pH 3 to 10, and proteolytic enzymes. P2 disrupted the cell membrane and caused bacteriolysis, in which its action was dependent on the incubation time and peptide concentration. Antibiofilm activity of P2 was determined by which the half-maximal inhibition of biofilm formation was observed at 2.92 and 4.84 µg/mL for S. aureus TISTR 517 and MRSA isolate 2468, respectively. Biofilm eradication of tested pathogens was found at the P2 concentration of 128 µg/mL. Furthermore, P2 hemolytic activity was less than 10% at concentrations up to 64 µg/mL, which reflected the hemolysis index thresholds of 32. Conclusion Five novel anti-MRSA peptides were identified from SPR19. P2 was the most active peptide and was demonstrated to cause membrane disruption and cell lysis. The P2 activity was dependent on the peptide concentration and exposure time. This peptide had antibiofilm activity against tested pathogens and was compatible with human erythrocytes, supporting its potential use as an anti-MRSA agent in this post-antibiotic era.

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Section: Discussionmentioning

confidence: 99%

Anti-methicillin-resistant Staphylococcus aureus and antibiofilm activity of new peptides produced by a Brevibacillus strain

Ogunsile,

Songnaka,

Sawatdee

et al. 2023

PeerJ

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“…The same holds for DOPC monolayers. Obviously, LL-20 cannot penetrate into zwitterionic lipid monolayers at physiologically relevant surface pressures (30)(31)(32)(33)(34)(35) mN/m), independent of the lipid phase. LL-32 has a slightly higher MIP of (35 2)mN/m into DPPC with a slope of −0.7, indicating an interaction with the zwitterionic DPPC at low lateral pressures.…”

Section: Interactions Of Ll-32 and Ll-20 With Pre-compressed Monolayersmentioning

confidence: 99%

“…It was shown that the peptides differ drastically in their surface activity (equilibrium adsorption pressure). As concluded from CD spectra, both peptides are unstructured in bulk but exhibit different secondary structures when adsorbed to the air/buffer interface [31,32]. While LL-32 transforms into an -helix lying flat at the buffer surface, with a helix diameter of 17 Å, LL-20 adopts a partly unstructured conformation.…”

Section: Introductionmentioning

confidence: 95%

Interactions of Two Fragments of the Human Antimicrobial Peptide LL-37 with Zwitterionic and Anionic Lipid Monolayers

Dannehl

Brezesinski

Möhwald

2014

Zeitschrift Für Physikalische Chemie

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The interactions of two fragments of the human antimicrobial LL-37 with lipid monolayers at the soft liquid/air interface have been characterized. To model the interaction with mammalian cell membranes, lipid monolayers composed of the zwitterionic DPPC and DOPC were used. To investigate the interaction with bacterial cell membranes, lipid monolayers of anionic DPPG and POPG were used. DPPC and DPPG exhibit a first-order phase transition from the disordered liquid to the ordered condensed state, whereas POPG and DOPC monolayers are in the fluid disordered state at all surface pressures studied. Therefore, the influence of the monolayer phase state on peptide-lipid interactions can be studied. To obtain insight into the peptide structure and their influence on phospholipid membranes, film balance measurements were coupled with surface sensitive Infrared Reflection-Absorption Spectroscopy (IRRAS). The results were compared to CD measurements in bulk. LL-32 is more surface active and can better intercalate into lipid monolayers than LL-20. Even though LL-32 has no cell-selectivity, our results show how the peptide interacts differently with zwitterionic compared to anionic membrane models. The interaction with DPPC monolayers is based on simple intercalation of the peptides between the lipid molecules. However, the peptides bind in a two-step process to DPPG monolayers, which results in a fluidization of the lipid film. This can be related to a membrane thinning.

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The interaction of antimicrobial peptides with membranes

Travkova

Moehwald

Brezesinski

2017

Advances in Colloid and Interface Science

160

112

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Effect of SDS and CTAB on Derivatives of Antimicrobial Peptides Arenicin and LL-37

Cited by 3 publications

References 21 publications

Anti-methicillin-resistant Staphylococcus aureus and antibiofilm activity of new peptides produced by a Brevibacillus strain

Anti-methicillin-resistant Staphylococcus aureus and antibiofilm activity of new peptides produced by a Brevibacillus strain

Interactions of Two Fragments of the Human Antimicrobial Peptide LL-37 with Zwitterionic and Anionic Lipid Monolayers

The interaction of antimicrobial peptides with membranes

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