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BBA - Biomembranes (v.1828, #6)

Editorial Board (pp. i).

Grazing Incidence X-ray Diffraction and Brewster Angle Microscopy studies on domain formation in phosphatidylethanolamine/cholesterol monolayers imitating the inner layer of human erythrocyte membrane by Paweł Wydro; Flasinski Michał Flasiński; Marcin Broniatowski (pp. 1415-1423).

In this work the properties of monomolecular films composed of 1-stearoyl-2-oleoyl- sn-glycero-3-phosphoethanolamine (SOPE) and cholesterol, differing in lipid proportion, were investigated in the context of domain formation in the inner leaflet of membrane. To perform comprehensive analysis of the studied model systems the Langmuir monolayer experiments were performed in combination with Brewster angle microscopy (BAM) and Grazing Incidence X-ray Diffraction (GIXD) techniques. The analysis of the collected data proved non-ideal behavior of the investigated films. It was found that cholesterol at its lower concentration in the system (10%) is of disturbing influence on SOPE film. Further addition of cholesterol into phospholipids film (33, 50, and 67% of cholesterol) induces an ordering effect on SOPE acyl chains and provokes the formation of sterol-poor and sterol-rich domains which stoichiometry is independent of monolayer composition. The foregoing findings allow one to conclude that in cytosolic leaflet of membrane the lipids may segregate into domains of various cholesterol contents which depending on their composition may play different roles in membrane functioning.Display Omitted► Molecular organization of artificial inner layer of human erythrocyte membrane ► Cholesterol concentration affects the morphology of phosphatidylethanolamine film. ► Cholesterol-poor and cholesterol-rich domains coexist in model membrane. ► Domain composition is independent of sterol concentration in the mixed monolayer.

Keywords: Phosphatidylethanolamine; Cholesterol; Model cytosolic layer; Domain formation

Low-flux electron diffraction study for the intercellular lipid organization on a human corneocyte by Hiromitsu Nakazawa; Tomohiro Imai; Ichiro Hatta; Shingo Sakai; Shintaro Inoue; Satoru Kato (pp. 1424-1431).

Human skin stratum corneum (SC) structures were investigated by electron diffraction (ED) with a very low-flux electron beam with the help of high-sensitivity detectors, the imaging plate and the CCD camera. This low-flux electron diffraction (LFED) method made it possible to minimize the unfavorable effect of electron beam damage and to give a reliable diffraction pattern from a small selected area (0.2μm²) on a corneocyte. Dependence of the 2-dimensional ED pattern on the size of the selected area showed that orientational correlation between lipid packing domains can persist over the area much larger than their domain size. The LFED method also allowed us to trace the detailed structural change induced by the electron beam damage. The ED diffraction peak for the lattice constant of about 4.1nm decayed in three steps. The detailed analysis of these three steps suggested that a different type of orthorhombic structure exists interacted with the well-described hexagonal and orthorhombic structures, in the process of decay resulting from electron beam damage.Display Omitted► Human SC were investigated by electron diffraction with a very low electron flux. ► This method allowed us to trace the detailed structural change by electron damage. ► The structural changes of SC suggested that 2 types of orthorhombic structures exist.

Keywords: Corneocyte; Intercellular lipid; Low-flux electron diffraction; Electron beam damage

Properties of membranes derived from the total lipids extracted from the human lens cortex and nucleus by Laxman Mainali; Marija Raguz; William J. O'Brien; Witold K. Subczynski (pp. 1432-1440).

Human lens lipid membranes prepared using a rapid solvent exchange method from the total lipids extracted from the clear lens cortex and nucleus of 41- to 60-year-old donors were investigated using electron paramagnetic resonance spin-labeling. Profiles of the phospholipid alkyl-chain order, fluidity, oxygen transport parameter, and hydrophobicity were assessed across coexisting membrane domains. Membranes prepared from the lens cortex and nucleus were found to contain two distinct lipid environments, the bulk phospholipid– cholesterol domain and the cholesterol bilayer domain (CBD). The alkyl chains of phospholipids were strongly ordered at all depths, indicating that the amplitude of the wobbling motion of alkyl chains was small. However, profiles of the membrane fluidity, which explicitly contain time (expressed as the spin-lattice relaxation rate) and depend on the rotational motion of spin labels, show relatively high fluidity of alkyl chains close to the membrane center. Profiles of the oxygen transport parameter and hydrophobicity have a rectangular shape and also indicate a high fluidity and hydrophobicity of the membrane center. The amount of CBD was greater in nuclear membranes than in cortical membranes. The presence of the CBD in lens lipid membranes, which at 37°C showed a permeability coefficient for oxygen about 60% smaller than across a water layer of the same thickness, would be expected to raise the barrier for oxygen transport across the fiber cell membrane. Properties of human membranes are compared with those obtained for membranes made of lipids extracted from cortex and nucleus of porcine and bovine eye lenses.Display Omitted► Physical properties of human cortical and nuclear lens lipid membranes ► Discriminated domains are phospholipid cholesterol and cholesterol bilayer domains. ► Presence of the cholesterol bilayer domain raises the barrier for oxygen transport.

Keywords: Cholesterol; Membrane domains; Fluidity; Hydrophobic barrier; Oxygen permeation; Spin labeling

Lipid interaction triggering Septin2 to assembly into β-sheet structures investigated by Langmuir monolayers and PM-IRRAS by Julio C.P. Damalio; Thatyane M. Nobre; Jose Luiz Lopes; Osvaldo N. Oliveira Jr.; Araujo Ana Paula U. Araújo (pp. 1441-1448).

The molecular mechanisms responsible for protein structural changes in the central nervous system leading to Alzheimer's disease are unknown, but there is evidence that a family of proteins known as septins may be involved. Septins are a conserved group of GTP-binding proteins which participate in various cellular processes, including polarity determination and membrane dynamics. SEPT1, SEPT4, and SEPT2 have been found in deposits known as neurofibrillary tangles and glial fibrils in Alzheimer's disease. In this study, we provide molecular-level information for the interaction of SEPT2 with Langmuir monolayers at the air/water interface, which are used as simplified membrane models. The high surface activity of SEPT2 causes it to adsorb onto distinct types of lipid Langmuir monolayers, namely dipalmitoylphosphatidylcholine and PtdIns(4,5)P₂. However, the interaction with PtdIns(4,5)P₂ is much stronger, not only leading to a higher adsorption, but also to SEPT2 remaining inserted within the membrane at high surface pressures. Most importantly, in situ polarization-modulated infrared reflection absorption spectroscopy results indicated that the native secondary structure of SEPT2 is preserved upon interacting with PtdIns(4,5)P₂, but not when dipalmitoylphosphatidylcholine is at the air/water interface. Taken together, the results presented here suggest that the interaction between SEPT2 and the cell membrane may play an important role in the assembly of SEPT2 into amyloid-like fibers.Display Omitted► Investigation of the binding of SEPT2 to PtdIns(4,5)P₂ and DPPC, using the Langmuir monolayer, DSC and PM-IRRAS techniques ► SEPT2 interacts with PtdIns(4,5)P₂, remaining incorporated in the monolayer and with its secondary structure preserved. ► The binding to DPPC could trigger SEPT2 assembly into amyloid fibrils. ► SEPT2 in amyloid filament conformation no longer interacts with PtdIns(4,5)P₂ in the Langmuir monolayer.

Keywords: Human septin 2; Langmuir monolayer; PM-IRRAS; Phospholipid; Amyloid

Synergistic action of Galleria mellonella apolipophorin III and lysozyme against Gram-negative bacteria by Agnieszka Zdybicka-Barabas; Staczek Sylwia Stączek; Paweł Mak; Krzysztof Skrzypiec; Ewaryst Mendyk; Cytrynska Małgorzata Cytryńska (pp. 1449-1456).

Insect immune response relies on the humoral and cellular mechanisms of innate immunity. The key factors are the antimicrobial polypeptides that act in concert against invading pathogens. Several such components, e.g. apolipophorin III (apoLp-III), lysozyme, and anionic peptide 2, are present constitutively in the hemolymph of non-challenged Galleria mellonella larvae. In the present study, we demonstrate an evidence for a synergistic action of G. mellonella lysozyme and apoLp-III against Gram-negative bacteria, providing novel insights into the mode of action of these proteins in insect antimicrobial defense. It was found that the muramidase activity of G. mellonella lysozyme considerably increased in the presence of apoLp-III. Moreover, apoLp-III enhanced the permeabilizing activity of lysozyme toward Escherichia coli cells. As shown using non-denaturing PAGE, the proteins did not form intermolecular complexes in vivo and in vitro, indicating that the effect observed was not connected with the intermolecular interactions between the proteins. Analysis of AFM images of E. coli cells exposed to G. mellonella lysozyme and/or apoLp-III revealed evident alterations in the bacterial surface structure accompanied by the changes in their biophysical properties. The bacterial cells demonstrated significant differences in elasticity, reflected by Young's modulus, as well as in adhesive forces and roughness values in comparison to the control ones. The constitutive presence of these two defense molecules in G. mellonella hemolymph and the fact that apoLp-III enhances lysozyme muramidase and perforating activities indicate that they can be regarded as important antibacterial factors acting at the early stage of infection against Gram-negative as well as Gram-positive bacteria. G. mellonella apolipophorin III enhances muramidase (A) and E. coli cell membrane permeabilizing (B) activity of lysozyme. E. coli cells exposed to G. mellonella lysozyme and apoLp-III exhibit changes in cell surface structure and properties as revealed by AFM analysis (C).Display Omitted► G. mellonella apoLp-III enhances lysozyme muramidase activity. ► G. mellonella apoLp-III enhances lysozyme perforating activity toward E. coli. ► G. mellonella apoLp-III and lysozyme alter structure of bacterial cell surface. ► G. mellonella apoLp-III and lysozyme alter properties of bacterial cell surface. ► G. mellonella apoLp-III and lysozyme do not form intermolecular complexes.

Keywords: Galleria mellonella; Apolipophorin III; Lysozyme; Atomic force microscopy

The enhanced membrane interaction and perturbation of a cell penetrating peptide in the presence of anionic lipids: Toward an understanding of its selectivity for cancer cells by Marie-Lise Jobin; Pierre Bonnafous; Hamza Temsamani; François Dole; Grelard Axelle Grélard; Erick J. Dufourc; Isabel D. Alves (pp. 1457-1470).

Cell penetrating peptides (CPPs) are usually short, highly cationic peptides that are capable of crossing the cell membrane and transport cargos of varied size and nature in cells by energy- and receptor-independent mechanisms. An additional potential is the newly discovered anti-tumor activity of certain CPPs, including RW16 (RRWRRWWRRWWRRWRR) which is derived from penetratin and is investigated here. The use of CPPs in therapeutics, diagnosis and potential application as anti-tumor agents increases the necessity of understanding their mode of action, a subject yet not totally understood. With this in mind, the membrane interaction and perturbation mechanisms of RW16 with both zwitterionic and anionic lipid model systems (used as representative models of healthy vs tumor cells) were investigated using a large panoply of biophysical techniques. It was shown that RW16 autoassociates and that its oligomerization state highly influences its membrane interaction. Overall a stronger association and perturbation of anionic membranes was observed, especially in the presence of oligomeric peptide, when compared to zwitterionic ones. This might explain, at least in part, the anti-tumor activity and so the selective interaction with cancer cells whose membranes have been shown to be especially anionic. Hydrophobic contacts between the peptide and lipids were also shown to play an important role in the interaction. That probably results from the tryptophan insertion into the fatty acid lipid area following a peptide flip after the first electrostatic recognition. A model is presented that reflects the ensemble of results.Display Omitted► RW16 is a CPP with reported activity on cancer cell mobility and proliferation. ► RW16 interaction with membranes mimicking healthy and cancer cells was investigated. ► Zwitterionic lipids mimic healthy cells and anionic lipid cancer cells. ► RW16 oligomerization occurs and affects the interaction with membranes. ► RW16 induced stronger association and perturbation of anionic membranes.

Keywords: Abbreviations; AMP; Anti-microbial peptide; APA; Amino pentanoic acid; CD; Circular dichroism; CHO; Chinese hamster ovary; CPP; Cell-penetrating peptide; DLS; Dynamic Light Scattering; DMPC; Dimyristoyl phosphatidylcholine; DMPG; Dimyristoyl phosphatidylglycerol; DOPC; Dioleoyl phosphatidylcholine; DOPE; Dioleoyl phosphatidylethanolamine; DOPG; Dioleoyl phosphatidylglycerol; DOPS; Dioleoyl phosphatidylserine; DPPC; Dipalmitoyl phosphatidylcholine; DSC; Differential Scanning Calorimetry; GUV; Giant Unilamellar Vesicle; ITC; Isothermal Titration Calorimetry; LUV; Large unilamellar vesicle; MIC; Minimal inhibitory concentration; MLV; Multilamellar vesicle; PC; Phosphatidylcholine; PE; Phosphatidylethanolamine; PG; Phosphatidylglycerol; PS; Phosphatidylserine; SAR; Structure–activity relationshipCell penetrating peptide; Peptide/lipid interaction; Lipid model system; Anticancer activity

Structural features of the apelin receptor N-terminal tail and first transmembrane segment implicated in ligand binding and receptor trafficking by David N. Langelaan; Tyler Reddy; Aaron W. Banks; Graham Dellaire; Dupre Denis J. Dupré; Jan K. Rainey (pp. 1471-1483).

G-protein coupled receptors (GPCRs) comprise a large family of membrane proteins with rich functional diversity. Signaling through the apelin receptor (AR or APJ) influences the cardiovascular system, central nervous system and glucose regulation. Pathophysiological involvement of apelin has been shown in atherosclerosis, cancer, human immunodeficiency virus-1 (HIV-1) infection and obesity. Here, we present the high-resolution nuclear magnetic resonance (NMR) spectroscopy-based structure of the N-terminus and first transmembrane (TM) segment of AR (residues 1–55, AR55) in dodecylphosphocholine micelles. AR55 consists of two disrupted helices, spanning residues D14-K25 and A29-R55^1.59. Molecular dynamics (MD) simulations of AR built from a hybrid of experimental NMR and homology model-based restraints allowed validation of the AR55 structure in the context of the full-length receptor in a hydrated bilayer. AR55 structural features were functionally probed using mutagenesis in full-length AR through monitoring of apelin-induced extracellular signal-regulated kinase (ERK) phosphorylation in transiently transfected human embryonic kidney (HEK) 293A cells. Residues E20 and D23 form an extracellular anionic face and interact with lipid headgroups during MD simulations in the absence of ligand, producing an ideal binding site for a cationic apelin ligand proximal to the membrane–water interface, lending credence to membrane-catalyzed apelin-AR binding. In the TM region of AR55, N46^1.50 is central to a disruption in helical character. G42^1.46, G45^1.49 and N46^1.50, which are all involved in the TM helical disruption, are essential for proper trafficking of AR. In summary, we introduce a new correlative NMR spectroscopy and computational biochemistry methodology and demonstrate its utility in providing some of the first high-resolution structural information for a peptide-activated GPCR TM domain.Display Omitted► We present the structure of the N-terminal portion of the human apelin receptor (AR). ► Combining NMR data and MD simulation, we place this in the full-length AR context. ► The first transmembrane helix of AR is a kinked helix and is required for trafficking. ► The AR N-terminal tail has an anionic surface ideal for binding its ligand, apelin. ► This is one of the first structural characterizations of a peptide-activated GPCR.

Keywords: Abbreviations; AR; apelin receptor; AR55; residues 1–55 of AR; BSA; bovine serum albumin; CSI; chemical shift index; DMEM; Dulbecco's modified eagle medium; DPC; dodecylphosphocholine; DPPC; dipalmitoylphosphatidylcholine; DSS; sodium 2,2-dimethyl-2-silapentane-5-sulfonate; DTT; dithitothreitol; ERK; extracellular signal-regulated kinase; FBS; fetal bovine serum; GPCR; G-protein coupled receptor; HA; hemagglutinin; HEK; human embryonic kidney; HSQC; heteronuclear single quantum coherence; IPTG; isopropyl β-D-1-thiogalactopyranoside; LB; Luria broth; MD; molecular dynamics; NMR; nuclear magnetic resonance; NOE; nuclear Overhauser enhancement; NOESY; NOE spectroscopy; PCR; polymerase chain reaction; PEI; polyethylenimine; PDB; Protein Data Bank; RMSD; root mean square deviation; TFA; trifluoracetic acid; TM; transmembrane; TOCSY; total correlation spectroscopyApelin receptor; Membrane protein structure; Divide and conquer; Biomolecular NMR spectroscopy; Homology model; Molecular dynamics simulations

Different roles of cell surface and exogenous glycosaminoglycans in controlling gene delivery by arginine-rich peptides with varied distribution of arginines by Rangeetha J. Naik; Anindo Chatterjee; Munia Ganguli (pp. 1484-1493).

The role of cell surface and exogenous glycosaminoglycans (GAGs) in DNA delivery by cationic peptides is controlled to a large extent by the peptide chemistry and the nature of its complex with DNA. We have previously shown that complexes formed by arginine homopeptides with DNA adopt a GAG-independent cellular internalization mechanism and show enhanced gene delivery in presence of exogenous GAGs. In contrast, lysine complexes gain cellular entry primarily by a GAG-dependent pathway and are destabilized by exogenous GAGs. The aim of the current study was to elucidate the factors governing the role of cell surface and soluble glycosaminoglycans in DNA delivery by sequences of arginine-rich peptides with altered arginine distributions (compared to homopeptide). Using peptides with clustered arginines which constitute known heparin-binding motifs and a control peptide with arginines alternating with alanines, we show that complexes formed by these peptides do not require cell surface GAGs for cellular uptake and DNA delivery. However, the charge distribution and the spacing of arginine residues affects DNA delivery efficiency of these peptides in presence of soluble GAGs, since these peptides show only a marginal increase in transfection in presence of exogenous GAGs unlike that observed with arginine homopeptides. Our results indicate that presence of arginine by itself drives these peptides to a cell surface GAG-independent route of entry to efficiently deliver functional DNA into cells in vitro. However, the inherent stability of the complexes differ when the distribution of arginines in the peptides is altered, thereby modulating its interaction with exogenous GAGs.Display Omitted► Analyzing role of glycosaminoglycans in gene delivery is crucial for designing efficient carriers. ► DNA delivery by arginine-rich peptides does not require cell surface glycosaminoglycans. ► Contiguous arginines show maximum stability in presence of exogenous glycosaminoglycans. ► Distribution of arginines controls DNA delivery with exogenous glycosaminoglycans.

Keywords: Abbreviations; GAG; glycosaminoglycan; CHO; Chinese hamster ovary; PBS; phosphate buffered saline; FITC; fluorescein isothiocyanate; EtBr; ethidium bromide; AFM; atomic force microscopy; HS; heparan sulfate; CS; chondroitin sulfate; C6S; chondroitin 6-sulfateGene delivery; Arginine peptides; Glycosaminoglycans; Heparin-binding motif; Peptide-DNA complex

An NMR investigation of the structure, function and role of the hERG channel selectivity filter in the long QT syndrome by Andrée E. Gravel; Alexandre A. Arnold; Erick J. Dufourc; Isabelle Marcotte (pp. 1494-1502).

The human ether-a-go-go-related gene (hERG) voltage-gated K⁺ channels are located in heart cell membranes and hold a unique selectivity filter (SF) amino acid sequence (SVGFG) as compared to other K⁺ channels (TVGYG). The hERG provokes the acquired long QT syndrome (ALQTS) when blocked, as a side effect of drugs, leading to arrhythmia or heart failure. Its pore domain – including the SF – is believed to be a cardiotoxic drug target. In this study combining solution and solid-state NMR experiments we examine the structure and function of hERG's L⁶²²-K⁶³⁸ segment which comprises the SF, as well as its role in the ALQTS using reported active drugs. We first show that the SF segment is unstructured in solution with and without K⁺ ions in its surroundings, consistent with the expected flexibility required for the change between the different channel conductive states predicted by computational studies. We also show that the SF segment has the potential to perturb the membrane, but that the presence of K⁺ ions cancels this interaction. The SF moiety appears to be a possible target for promethazine in the ALQTS mechanism, but not as much for bepridil, cetirizine, diphenhydramine and fluvoxamine. The membrane affinity of the SF is also affected by the presence of drugs which also perturb model DMPC-based membranes. These results thus suggest that the membrane could play a role in the ALQTS by promoting the access to transmembrane or intracellular targets on the hERG channel, or perturbing the lipid–protein synergy.Display Omitted•hERG's L⁶²²-K⁶³⁸ segment comprising the selectivity filter is unstructured in water.•This segment has the potential to perturb the lipid membrane.•Its membrane affinity is affected by K⁺ ions and drugs.•It is a potential target for promethazine in the ALQTS mechanism.•Non-specific drug–membrane interactions could play a role in the ALQTS.

Keywords: Human ether-a-go-go-related gene; Phosphatidylcholine model membrane; Lipid bicelle; Multilamellar vesicle; Nuclear magnetic resonance; Cardiotoxic drugs

Apolipoprotein A–I binding to anionic vesicles and lipopolysaccharides: Role for lysine residues in antimicrobial properties by Wendy H.J. Beck; Christopher P. Adams; Ivan M. Biglang-awa; Arti B. Patel; Heather Vincent; Eric J. Haas-Stapleton; Paul M.M. Weers (pp. 1503-1510).

Human apolipoprotein A–I (apoA–I) is a 28kDa protein and a major component of high-density lipoproteins, mediating several essential metabolic functions related to heart disease. In the present study the potential protective role against bacterial pathogens was explored. ApoA–I suppressed bacterial growth of Escherichia coli and Klebsiella pneumoniae. The protein was able to bind lipopolysaccharides and showed a strong preference for bilayer vesicles made of phosphatidylglycerol over phosphatidylcholine. Lysine side chains of apoA–I were acetylated to evaluate the importance of electrostatic forces in the binding interaction with both membrane components. Electrophoresis properties, dot blot analysis, circular dichroism, and fluorescence spectroscopy to probe for changes in protein structure indicated that the acetylated protein displayed a strongly reduced lipopolysaccharide and phosphatidylglycerol binding. A mutant containing only the N-terminal domain of apoA–I also showed a reduced ability to interact with the membrane components, although to a lesser extent. These results indicate the potential for apoA–I to function as an antimicrobial protein and exerts this function through lysine residues.Display Omitted► apoA–I binding to LPS was strongly reduced upon acetylation of lysine residues. ► apoA–I shows a much stronger binding interaction with PG compared to PC. ► Acetylated protein lost most of the PG binding activity. ► Antimicrobial activity was reduced for acetylated apoA–I. ► Electrostatic forces are critical for binding of apoA–I to LPS and PG.

Keywords: Abbreviations; ANS; 8-anilinonaphthalene-1-sulfonate; apoA–I; apolipoprotein A–I; BSA; bovine serum albumin; CD; circular dichroism; CFU; colony forming units; HDL; high-density lipoproteins; LPS; lipopolysaccharides; PC; phosphatidylcholine; PG; phosphatidylglycerol; PBS; phosphate buffered saline; LUV; large unilamellar vesicles; TBS; Tris buffered saline; WT; wild-typeApolipoprotein; apoA–I; Lipopolysaccharides; Phosphatidylglycerol; Antimicrobial

Real-time attack of LL-37 on single Bacillus subtilis cells by Kenneth J. Barns; James C. Weisshaar (pp. 1511-1520).

Time-lapse fluorescence microscopy of single, growing Bacillus subtilis cells with 2–12s time resolution reveals the mechanisms of antimicrobial peptide (AMP) action on a Gram-positive species with unprecedented detail. For the human cathelicidin LL-37 attacking B. subtilis, the symptoms of antimicrobial stress differ dramatically depending on the bulk AMP concentration. At 2μM LL-37, the mean single-cell growth rate decreases, but membrane permeabilization does not occur. At 4μM LL-37, cells abruptly shrink in size at the same time that Sytox Green enters the cytoplasm and stains the nucleoids. We interpret the shrinkage event as loss of turgor pressure (and presumably the membrane potential) due to permeabilization of the membrane. Movies of Sytox Green staining at 0.5frame/s show that nucleoid staining is initially local, more consistent with pore formation than with global permeabilization models. In a novel “growth recovery” assay, cells are incubated with LL-37 for a variable period and then rinsed with fresh growth medium lacking LL-37. The growth rate attenuation observed at 2μM LL-37 is a recoverable symptom, while the abrupt cell shrinkage observed at 4μM LL-37 is not.Display Omitted► Time-lapse images of Bacillus subtilis were obtained during exposure to LL-37. ► Cells exposed to 2μM LL-37 show growth rate attenuation but no membrane disruption. ► Cells exposed to 4μM LL-37 abruptly shrink and exhibit membrane disruption. ► Nucleoid staining by Sytox Green suggests localized membrane disruption. ► Symptoms at 2μM LL-37 are recoverable, while symptoms at 4μM LL-37 are not.

Keywords: Abbreviations; AMP; Antimicrobial peptide; GFP; Green fluorescent protein; MIC; Minimum inhibitory concentration; MBC; Minimum bactericidal concentration; FWHM; Full-width half maximum Bacillus subtilis; Antimicrobial peptide; LL-37; Fluorescence microscopy

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BBA - Biomembranes (v.1828, #6)