Effect of Liposome Surface Charge and Peptide Side Chain Charge Density on Antimicrobial Peptide-Membrane Binding as Determined by Circular Dichroism

Urushibara, Takafumi

doi:10.4172/2155-9589.1000124

Cited by 6 publications

(12 citation statements)

References 53 publications

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“…How the peptides interact with the membranes depends on the sequence, structure and concentration of the peptide and composition of the membrane [ 8 ]. We selected membrane-active CPPs and AMPs, focusing on peptides that most probably adopt the active structure while surrounded by lipids.…”

Section: Introductionmentioning

confidence: 99%

“…Generally, the selectivity of peptides towards different membranes depends on the chemical composition of the membranes, which differs among bacteria [ 8 , 30 , 31 ]. Positively charged peptides interact with high affinity with the membranes containing negatively charged lipids, while their binding to neutral membranes is weak [ 31 ].…”

Section: Introductionmentioning

confidence: 99%

“…Eukaryotic membranes contain higher concentrations of heterogeneous phospholipids than membranes of prokaryotic organisms, such as bacteria with high content of negatively charged phospholipids [ 3 , 31 ]. Biological membranes are complex, so most studies of the peptide-membrane interactions are performed using membrane models [ 8 , 31 , 32 ]. The advantage of using simplified membrane models is that the influence of each lipid can be tested separately.…”

Section: Introductionmentioning

confidence: 99%

“…POPE differs from POPC by the absence of three methyl groups at the nitrogen atom ( Figure 1 ) [ 34 ]. The POPC:POPE or POPC:POPG mixtures, in a molar ratio of 3:1, form SUV liposomes making them resemble, respectively, eukaryotic and prokaryotic membranes [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

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Conformational Changes of Anoplin, W-MreB1–9, and (KFF)3K Peptides near the Membranes

Wojciechowska

Miszkiewicz

Trylska

2020

IJMS

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Many peptides interact with biological membranes, but elucidating these interactions is challenging because cellular membranes are complex and peptides are structurally flexible. To contribute to understanding how the membrane-active peptides behave near the membranes, we investigated peptide structural changes in different lipid surroundings. We focused on two antimicrobial peptides, anoplin and W-MreB1–9, and one cell-penetrating peptide, (KFF)3K. Firstly, by using circular dichroism spectroscopy, we determined the secondary structures of these peptides when interacting with micelles, liposomes, E. coli lipopolysaccharides, and live E. coli bacteria. The peptides were disordered in the buffer, but anoplin and W-MreB1–9 displayed lipid-induced helicity. Yet, structural changes of the peptide depended on the composition and concentration of the membranes. Secondly, we quantified the destructive activity of peptides against liposomes by monitoring the release of a fluorescent dye (calcein) from the liposomes treated with peptides. We observed that only for anoplin and W-MreB1–9 calcein leakage from liposomes depended on the peptide concentration. Thirdly, bacterial growth inhibition assays showed that peptide conformational changes, evoked by the lipid environments, do not directly correlate with the antimicrobial activity of the peptides. However, understanding the relation between peptide structural properties, mechanisms of membrane disruption, and their biological activities can guide the design of membrane-active peptides.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Conformational Changes of Anoplin, W-MreB1–9, and (KFF)3K Peptides near the Membranes

Wojciechowska

Miszkiewicz

Trylska

2020

IJMS

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“…The other peptides remained mainly unstructured under any condition. Previously, it was demonstrated that the mechanism of action of AMPs is dependent on the surface charge and hydrophobicity of liposomes of mixed phospholipid compositions [ 42 ]. The secondary structure of the peptide changes under interactions with bacteria and can vary with different lipid membrane compositions.…”

Section: Discussionmentioning

confidence: 99%

The Hirudo Medicinalis Microbiome Is a Source of New Antimicrobial Peptides

Grafskaia

Pavlova

Babenko

et al. 2020

IJMS

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Antimicrobial peptides (AMPs) are considered a promising new class of anti-infectious agents. This study reports new antimicrobial peptides derived from the Hirudo medicinalis microbiome identified by a computational analysis method applied to the H. medicinalis metagenome. The identified AMPs possess a strong antimicrobial activity against Gram-positive and Gram-negative bacteria (MIC range: 5.3 to 22.4 μM), including Staphylococcus haemolyticus, an opportunistic coagulase–negative pathogen. The secondary structure analysis of peptides via CD spectroscopy showed that all the AMPs except pept_352 have mostly disordered structures that do not change under different conditions. For peptide pept_352, the α–helical content increases in the membrane environment. The examination of the mechanism of action of peptides suggests that peptide pept_352 exhibits a direct membranolytic activity. Furthermore, the cytotoxicity assay demonstrated that the nontoxic peptide pept_1545 is a promising candidate for drug development. Overall, the analysis method implemented in the study may serve as an effective tool for the identification of new AMPs.

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Unlike dengue virus, the conserved 14–23 residues in N-terminal region of Zika virus capsid is not involved in lipid interactions

Saumya

Kumar

et al. 2020

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Effect of Liposome Surface Charge and Peptide Side Chain Charge Density on Antimicrobial Peptide-Membrane Binding as Determined by Circular Dichroism

Cited by 6 publications

References 53 publications

Conformational Changes of Anoplin, W-MreB1–9, and (KFF)3K Peptides near the Membranes

Conformational Changes of Anoplin, W-MreB1–9, and (KFF)3K Peptides near the Membranes

The Hirudo Medicinalis Microbiome Is a Source of New Antimicrobial Peptides

Unlike dengue virus, the conserved 14–23 residues in N-terminal region of Zika virus capsid is not involved in lipid interactions

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