Interaction of a synthetic antimicrobial peptide with a model bilayer platform mimicking bacterial membranes

2017 ◽  
Vol 12 (4) ◽  
pp. 04E404 ◽  
Author(s):  
Lifang Niu ◽  
Thorsten Wohland ◽  
Wolfgang Knoll ◽  
Ingo Köper
Keyword(s):  
Antimicrobial Peptide ◽  
Bacterial Membranes

Interactions of the Antimicrobial Peptide Maculatin 1.1 and Analogues with Phospholipid Bilayers

2011 ◽  
Vol 64 (6) ◽  
pp. 798 ◽  
Author(s):  
David I. Fernandez ◽  
Marc-Antoine Sani ◽  
Frances Separovic
Keyword(s):  
Antimicrobial Peptide ◽  
Solid State Nmr ◽  
Acyl Chain ◽  
Head Group ◽  
Group Interactions ◽  
Bacterial Membranes ◽  
Helical Content ◽  
Lipid System ◽  
Acyl Chains ◽  
Mixed Bilayer

The interactions of the antimicrobial peptide, maculatin 1.1 (GLFGVLAKVAAHVVPAIAEHF-NH2) and two analogues, with model phospholipid membranes have been studied using solid-state NMR and circular dichroism spectroscopy. Maculatin 1.1 and the P15G and P15A analogues displayed minimal secondary structure in water, but with zwitterionic dimyristoylphosphatidylcholine (DMPC) vesicles displayed a significant increase in α-helical content. In mixed phospholipid vesicles of DMPC and anionic dimyristoylphosphatidylglycerol (DMPG), each peptide was highly structured with ~80% α-helical content. In DMPC vesicles, the native peptide displayed moderate head group interaction and significant perturbation of the lipid acyl chains. In DMPC/DMPG vesicles, maculatin 1.1 promoted formation of a DMPG-enriched phase and moderately increased disorder towards acyl chain ends of DMPC in the mixed bilayer. Both analogues showed reduced phospholipid head group interactions with DMPC but displayed significant interactions with the mixed lipid system. These effects support the preferential activity of these antimicrobial peptides for bacterial membranes.

scholarly journals Interaction of antimicrobial peptide Plantaricin149a and four analogs with lipid bilayers and bacterial membranes

2013 ◽  
Vol 44 (4) ◽  
pp. 1291-1298 ◽  
Author(s):  
José Luiz de Souza Lopes ◽  
Denise Cavalcante Hissa ◽  
Vânia Maria Maciel Melo ◽  
Leila Maria Beltramini
Keyword(s):  
Antimicrobial Peptide ◽  
Lipid Bilayers ◽  
Bacterial Membranes

scholarly journals Proteomic Adaptation of Streptococcus pneumoniae to the Antimicrobial Peptide Human Beta Defensin 3 (hBD3) in Comparison to Other Cell Surface Stresses

2020 ◽  
Vol 8 (11) ◽  
pp. 1697
Author(s):  
Pierre-Alexander Mücke ◽  
Anne Ostrzinski ◽  
Sven Hammerschmidt ◽  
Sandra Maaß ◽  
Dörte Becher
Keyword(s):  
Streptococcus Pneumoniae ◽  
Cell Surface ◽  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Specific Cell ◽  
Similar Response ◽  
Respiratory Pathogens ◽  
Human Respiratory Tract ◽  
Bacterial Membranes ◽  
Surface Stresses

The antimicrobial peptide human Beta defensin 3 (hBD3) is an essential part of the innate immune system and is involved in protection against respiratory pathogens by specifically permeabilizing bacterial membranes. The Gram-positive bacterium Streptococcus pneumoniae causes serious diseases including pneumonia, meningitis, and septicemia, despite being frequently exposed to human defense molecules, including hBD3 during colonization and infection. Thus, the question arises how pneumococci adapt to stress caused by antimicrobial peptides. We addressed this subject by analyzing the proteome of S. pneumoniae after treatment with hBD3 and compared our data with the proteomic changes induced by LL-37, another crucial antimicrobial peptide present in the human respiratory tract. As antimicrobial peptides usually cause membrane perturbations, the response to the membrane active cationic detergent cetyltrimethylammonium bromide (CTAB) was examined to assess the specificity of the pneumococcal response to antimicrobial peptides. In brief, hBD3 and LL-37 induce a similar response in pneumococci and especially, changes in proteins with annotated transporter and virulence function have been identified. However, LL-37 causes changes in the abundance of cell surface modification proteins that cannot be observed after treatment with hBD3. Interestingly, CTAB induces unique proteomic changes in S. pneumoniae. Though, the detergent seems to activate a two-component system that is also activated in response to antimicrobial peptide stress (TCS 05). Overall, our data represent a novel resource on pneumococcal adaptation to specific cell surface stresses on a functional level. This knowledge can potentially be used to develop strategies to circumvent pneumococcal resistance to antimicrobial peptides.

scholarly journals Antimicrobial Peptide Recognition of Bacterial Membranes

2011 ◽  
Vol 100 (3) ◽  
pp. 334a
Author(s):  
Marc-Antoine Sani ◽  
David I. Fernandez ◽  
John D. Gehman ◽  
Frances Separovic
Keyword(s):  
Antimicrobial Peptide ◽  
Peptide Recognition ◽  
Bacterial Membranes

scholarly journals Heterologous Expression and Purification of the Antimicrobial Peptide Buforin II

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Boda Ferenc-András ◽  
Szabó Zoltán-István ◽  
Szőcs Erika ◽  
Salamon Pál ◽  
Orbán Csongor ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Heterologous Expression ◽  
Antimicrobial Peptide ◽  
Solid Phase ◽  
Host Cells ◽  
Fusion Partner ◽  
Monitoring And Control ◽  
Expression And Purification ◽  
Recombinant Peptide ◽  
Bacterial Membranes

AbstractAntimicrobial peptides are natural substances that have played a role in the development of the adaptive immune system, and are currently involved in the prevention of infections, through their direct antimicrobial and immunomodulatory properties. While the amino acid composition and spatial structure vary, most antibacterial peptides have a positive surface charge, which allows them to bind to the negative bacterial membranes. Buforin II is a widely studied antimicrobial peptide first obtained through the structural modification of buforin I, a peptide isolated from Bufo gargarizans. The peptide showed significant antibacterial activity against Gram-positive and Gram-negative bacterial strains. The mechanism of action of buforin II differs from that of other antimicrobial peptides, as it binds directly to bacterial DNA and RNA. The aim of our study was to obtain recombinant buforin II with a ubiquitin fusion partner, through heterologous expression in Escherichia coli Rosetta™ (DE3)pLysS cells, using a laboratory scale biore-actor. The incubation of expression host cells in a bioreactor allowed the constant monitoring and control of the process parameters, leading to high biomass levels and an increased production rate of the peptide. The parameters used during incubation were: 37°C, pH=6.9 and dissolved oxygen level above 40%. Purification of the recombinant protein was accomplished by affinity chromatography using a Ni-chelate solid phase to which the 10xHistag of our construct showed affinity. Method optimisation consisted in the use of gradient and linear elution, of which the latter was found to be more effective. Digestion of the fusion partner from the target peptide was performed with ubiquitin carboxyl-terminal hydrolase enzyme. The expression and purification protocols developed in our experiment allow the production of a significant amount of buforin II, allowing its use for further research. Furthermore, the presented methods could be suitable for industrial production of the recombinant peptide..

scholarly journals Effects of Antibacterial Peptide F1 on Bacterial Liposome Membrane Integrity

2021 ◽  
Vol 8 ◽  
Author(s):  
Qun Wang ◽  
Bo Peng ◽  
Mingyue Song ◽  
Abdullah ◽  
Jun Li ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Membrane Structure ◽  
Bacterial Membrane ◽  
Phospholipid Membranes ◽  
Phospholipid Membrane ◽  
Gram Positive ◽  
Liposome Membrane ◽  
Gram Negative ◽  
Bacterial Membranes ◽  
Gram Positive Bacteria

Previous studies from our lab have shown that the antimicrobial peptide F1 obtained from the milk fermentation by Lactobacillus paracasei FX-6 derived from Tibetan kefir was different from common antimicrobial peptides; specifically, F1 simultaneously inhibited the growth of Gram-negative and Gram-positive bacteria. Here, we present follow-on work demonstrating that after the antimicrobial peptide F1 acts on either Escherichia coli ATCC 25922 (E. coli) or Staphylococcus aureus ATCC 63589 (S. aureus), their respective bacterial membranes were severely deformed. This deformation allowed leakage of potassium and magnesium ions from the bacterial membrane. The interaction between the antimicrobial peptide F1 and the bacterial membrane was further explored by artificially simulating the bacterial phospholipid membranes and then extracting them. The study results indicated that after the antimicrobial peptide F1 interacted with the bacterial membranes caused significant calcein leakage that had been simulated by different liposomes. Furthermore, transmission electron microscopy observations revealed that the phospholipid membrane structure was destroyed and the liposomes presented aggregation and precipitation. Quartz Crystal Microbalance with Dissipation (QCM-D) results showed that the antimicrobial peptide F1 significantly reduced the quality of liposome membrane and increased their viscoelasticity. Based on the study's findings, the phospholipid membrane particle size was significantly increased, indicating that the antimicrobial peptide F1 had a direct effect on the phospholipid membrane. Conclusively, the antimicrobial peptide F1 destroyed the membrane structure of both Gram-negative and Gram-positive bacteria by destroying the shared components of their respective phospholipid membranes which resulted in leakage of cell contents and subsequently cell death.

scholarly journals Investigation of the role of aromatic residues in the antimicrobial peptide BuCATHL4B

2020 ◽  
Vol 27 ◽  
Author(s):  
Matthew R. Necelis ◽  
Luis E. Santiago-Ortiz ◽  
Gregory A. Caputo
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptide ◽  
Lipid Bilayers ◽  
Aromatic Amino Acids ◽  
Membrane Permeabilization ◽  
Peptide Sequence ◽  
Lipid Vesicle ◽  
Attractive Alternative ◽  
Bacterial Membranes

Background: Antimicrobial Peptides (AMPs) are an attractive alternative to traditional small molecule antibiotics as AMPs typically target the bacterial cell membrane. A Trp-rich peptide sequence derived from water buffalo (Bubalus bubalis), buCATHL4B was previously identified as a broad-spectrum antimicrobial peptide. Objective: In this work, native Trp residues were replaced with other naturally occurring aromatic amino acids to begin to elucidate the importance of these residues on peptide activity. Methods: Minimal Inhibitory Concentration (MIC) results demonstrated activity against seven strains of bacteria. Membrane and bilayer permeabilization assays were performed to address the role of bilayer disruption in the activity of the peptides. Lipid vesicle binding and quenching experiments were also performed to gain an understanding of how the peptides interacted with lipid bilayers. Results: MIC results indicate the original, tryptophan-rich sequence, and the phenylalanine substituted sequences exhibit strong inhibition of bacterial growth. In permeabilization assays, peptides with phenylalanine substitutions have higher levels of membrane permeabilization than those substituted with tyrosine. In addition, one of the two-tyrosine substituted sequence, YWY, behaves most differently in the lowest antimicrobial activity, showing no permeabilization of bacterial membranes. Notably the antimicrobial activity is inherently species dependent, with varying levels of activity against different bacteria. Conclusion: There appears to be little correlation between membrane permeabilization and activity, indicating these peptides may have additional mechanisms of action beyond membrane disruption. The results also identify two sequences, denoted FFF and YYW, which retain antibacterial activity but have markedly reduced hemolytic activity.

scholarly journals Identification of an antimicrobial peptide from large freshwater snail (Lymnaea stagnalis): activity against antibiotics resistant Staphylococcus epidermidis

2016 ◽  
Vol 2 ◽  
pp. 5-9
Author(s):  
Samiran Sona Gauri ◽  
◽  
Chandan Kumar Bera ◽  
Rabindranath Bhattacharyya ◽  
Santi Mohan Mandal ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Staphylococcus Epidermidis ◽  
Lymnaea Stagnalis ◽  
Public Health Problem ◽  
Freshwater Snail ◽  
Reversed Phase ◽  
Bacterial Membranes ◽  
Wide Range ◽  
Phase Liquid ◽  
Conventional Antibiotics

Nowadays, antibiotic resistance in bacteria is a great public health problem of increasing magnitude due to quick evolution through mutation that has generated the urgency to find the effective solutions to address this problem. Aside the conventional antibiotics, antimicrobial peptides are a new class of antimicrobials is known to have the activity against a wide range of bacteria. An antimicrobial peptide was isolated and purified from the Lymnaea stagnalis, a fresh water large snail, using ultrafiltration and reversed phase liquid chromatography. The molecular mass of the peptide 2345 Da was determined using MALDI TOF mass spectrometry. This peptide is efficiently prevented the growth of Staphylococcus epidermidis that resistant to ampicillin and chloramphenicol antibiotics. The MIC value was 16 μg/mL and specifically damage to bacterial membranes. Hence, this reported peptide revealed an alternative candidate to controlling the Staphylococcal infections.

Interaction of the antimicrobial peptide melimine with bacterial membranes

2010 ◽  
Vol 35 (6) ◽  
pp. 566-572 ◽  
Author(s):  
R. Rasul ◽  
N. Cole ◽  
D. Balasubramanian ◽  
R. Chen ◽  
N. Kumar ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Bacterial Membranes
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