Biochimica et biophysica acta. Biomembranes最新文献

{"title":"Monitoring the interactions between POPG phospholipid bilayer and amyloid-forming protein human cystatin C. Does the bilayer influence the oligomeric state and structure of the protein?","authors":"Przemyslaw Jurczak ,&nbsp;Igor Zhukov ,&nbsp;Marta Orlikowska ,&nbsp;Paulina Czaplewska ,&nbsp;Emilia Sikorska","doi":"10.1016/j.bbamem.2024.184285","DOIUrl":"10.1016/j.bbamem.2024.184285","url":null,"abstract":"<div><p><span>A biological membrane<span><span> is a structure characteristic for various cells and organelles present in almost all living organisms. Even though, it is one of the most common structures in organisms, where it serves crucial functions, a phospholipid bilayer may also take part in pathological processes leading to severe diseases. Research indicates that biological membranes have a profound impact on the pathological processes of </span>oligomerization<span> of amyloid-forming proteins. These processes are a hallmark of amyloid diseases, a group of pathological states involving, e.g., Parkinson's or Alzheimer's disease. Even though amyloidogenic diseases reap the harvest in modern societies, especially in elderly patients, the mechanisms governing the amyloid deposition are not clearly described. Therefore, the presented study focuses on the description of interactions between a model biological membrane (POPG) and one of amyloid forming proteins – human cystatin C. For the purpose of the study molecular dynamics simulations were applied to confirm interactions between the protein and POPG membrane. Next the NMR techniques were used to verify how the data obtained in solution compared to MD simulations and determine fragments of the protein responsible for interactions with POPG. Finally, </span></span></span>circular dichroism<span> was used to monitor the changes in secondary structure of the protein and size exclusion chromatography was used to monitor its oligomerization process. Obtained data indicates that the protein interacts with POPG submerging itself into the bilayer with the AS region. However, the presence of POPG bilayer does not significantly affect the structure or oligomerization process of human cystatin C.</span></p></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":null,"pages":null},"PeriodicalIF":3.4,"publicationDate":"2024-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139475065","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The enigmatic mode of action of the lantibiotic epilancin 15X","authors":"Xiaoqi Wang ,&nbsp;Yang Xu ,&nbsp;Nathaniel I. Martin ,&nbsp;Eefjan Breukink","doi":"10.1016/j.bbamem.2024.184282","DOIUrl":"https://doi.org/10.1016/j.bbamem.2024.184282","url":null,"abstract":"<div><p>Epilancin 15X is a lantibiotic that has an antimicrobial activity in the nanomolar concentration range towards <em>Staphylococcus simulans</em>. Such low MICs usually imply that these peptides employ a mechanism of action (MoA) involving high affinity targets. Here we studied this MoA by using epilancin 15X's ability to dissipate the membrane potential of intact <em>S. simulans</em> cells. These membrane depolarization assays showed that treatment of the bacteria by antibiotics known to affect the bacterial cell wall synthesis pathway decreased the membrane depolarization effects of epilancin 15X. Disruption of the Lipid II cycle in intact bacteria using several methods led to a decrease in the activity of epilancin 15X. Antagonism-based experiments on 96-well plate and agar diffusion plate pointed towards a possible interaction between epilancin 15X and Lipid II and this was confirmed by Circular Dichroism (CD) based experiments. However, this interaction did not lead to a detectable effect on either carboxyfluorescein (CF) leakage or proton permeability. All experiments point to the involvement of a phosphodiester-containing target within a polyisoprene-based biosynthesis pathway, yet the exact identity of the target remains obscure so far.</p></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":null,"pages":null},"PeriodicalIF":3.4,"publicationDate":"2024-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0005273624000130/pdfft?md5=19baddb1ac968b643687a53f19be383e&pid=1-s2.0-S0005273624000130-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139436012","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Probing amino acid side chains of the integral membrane protein PagP by solution NMR: Side chain immobilization facilitates association of secondary structures","authors":"Shaista Goel ,&nbsp;M. Rafid Feisal ,&nbsp;Gaddafi I. Danmaliki ,&nbsp;Shaohui Yu ,&nbsp;Philip B. Liu ,&nbsp;Russell E. Bishop ,&nbsp;Frederick G. West ,&nbsp;Peter M. Hwang","doi":"10.1016/j.bbamem.2024.184281","DOIUrl":"10.1016/j.bbamem.2024.184281","url":null,"abstract":"<div><p>Solution NMR spectroscopy of large protein systems is hampered by rapid signal decay, so most multidimensional studies focus on long-lived ¹H-¹³C magnetization in methyl groups and/or backbone amide ¹H-¹⁵N magnetization in an otherwise perdeuterated environment. Herein we demonstrate that it is possible to biosynthetically incorporate additional ¹H-¹²C groups that possess long-lived magnetization using cost-effective partially deuterated or unlabeled amino acid precursors added to <em>Escherichia coli</em> growth media. This approach is applied to the outer membrane enzyme PagP in membrane-mimetic dodecylphosphocholine micelles.</p><p>We were able to obtain chemical shift assignments for a majority of side chain ¹H positions in PagP using nuclear Overhauser enhancements (NOEs) to connect them to previously assigned backbone ¹H-¹⁵N groups and newly assigned ¹H-¹³C methyl groups. Side chain methyl-to-aromatic NOEs were particularly important for confirming that the amphipathic α-helix of PagP packs against its eight-stranded β-barrel, as indicated by previous X-ray crystal structures.</p><p>Interestingly, aromatic NOEs suggest that some aromatic residues in PagP that are buried in the membrane bilayer are highly mobile in the micellar environment, like Phe138 and Phe159. In contrast, Tyr87 in the middle of the bilayer is quite rigid, held in place by a hydrogen bonded network extending to the surface that resembles a classic catalytic triad: Tyr87-His67-Asp61. This hydrogen bonded arrangement of residues is not known to have any catalytic activity, but we postulate that its role is to immobilize Tyr87 to facilitate packing of the amphipathic α-helix against the β-barrel.</p></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":null,"pages":null},"PeriodicalIF":3.4,"publicationDate":"2024-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0005273624000129/pdfft?md5=1dfde38b8b4927cb1b995e54b5b5ae34&pid=1-s2.0-S0005273624000129-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139463140","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The accumulation of methylated porphyrins in dormant cells of Mycolicibacterium smegmatis is accompanied by a decrease in membrane fluidity and an impede of the functioning of the respiratory chain","authors":"Ivan A. Gligonov ,&nbsp;Daria I. Bagaeva,&nbsp;Galina R. Demina,&nbsp;Galina N. Vostroknutova,&nbsp;Dmitriy S. Vorozhtsov,&nbsp;Arseny S. Kaprelyants,&nbsp;Alexander P. Savitsky,&nbsp;Margarita O. Shleeva","doi":"10.1016/j.bbamem.2024.184270","DOIUrl":"10.1016/j.bbamem.2024.184270","url":null,"abstract":"<div><p>Transition of <em>Mycolicibacterium smegmatis (Msm)</em> and <span><em>Mycobacterium tuberculosis</em></span> to dormancy <em>in vitro</em><span><span> is accompanied by an accumulation of free methylated forms of porphyrins (tetramethyl coproporphyrin – TMC) localized in the cell wall of dormant bacteria. A study of the </span>fluorescence anisotropy<span> of BODIPY based fluorescent probes<span> on individual cell level using confocal microscope revealed significant changes in this parameter for BODIPY FL C16 from 0.05 to 0.22 for vegetative and dormant </span></span></span><em>Msm</em> cells correspondingly. Similarly, the increase of TMC concentration in vegetative <em>Msm</em><span><span> cells grown in the presence of 5-aminolevulinic acid (a known inducer of porphyrin synthesis) resulted in an increase of BODIPY FL C16 anisotropy. These changes in TMC concentration and membrane fluidity were accompanied by an inhibition of the activity of the </span>respiratory chain measured by oxygen consumption and a reduction of the DCPIP redox acceptor. During the first 8 h of the reactivation of the dormant </span><em>Msm</em><span><span> cells, the porphyrin content and probe fluorescent anisotropy returned to the level for vegetative bacteria. We suggested that upon transition to dormancy, an accumulation of TMC in membranes leads to a decrease in membrane fluidity, resulting in an inhibition of the respiratory chain activity. However, direct interactions of TMC with membrane bound enzymes cannot also be excluded. This, in turn, may result in the down regulation of many metabolic energy-dependent reactions as a part of mechanisms accompanying the transition to a hypometabolic state of </span>mycobacteria.</span></p></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":null,"pages":null},"PeriodicalIF":3.4,"publicationDate":"2024-01-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139414974","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Oseltamivir phosphate interaction with model membranes","authors":"Adriána Čelková ,&nbsp;Alexander Búcsi ,&nbsp;Mária Klacsová ,&nbsp;Tomáš Fazekaš ,&nbsp;Juan Carlos Martínez ,&nbsp;Daniela Uhríková","doi":"10.1016/j.bbamem.2024.184273","DOIUrl":"10.1016/j.bbamem.2024.184273","url":null,"abstract":"<div><p><span><span>Oseltamivir<span><span> belongs to the neuraminidase inhibitors, developed against the influenza virus, and registered under the trademark Tamiflu. Despite its long-term acquaintance, there is limited information in the literature about its physicochemical and structural properties in a lipid-water system. We present an experimentally determined </span>partition coefficient<span><span> with structural information on the interaction of oseltamivir with the model membrane, its possible location, and its effect on the membrane thermodynamics. The hydrophobic part of the </span>lipid </span></span></span>bilayer<span> is affected to a moderate extent, which was proved by slight changes in thermal and structural properties. Hereby, interaction of oseltamivir with the phospholipid bilayer induces concentration dependent decrease of lateral pressure in the bilayer acyl chain region. Oseltamivir charges the bilayer surface positively, which results in the </span></span>zeta potential increase and changes in anisotropic properties studied by the polarised light microscopy. At the highest oseltamivir concentrations studied, the multilamellar structure is extensively disturbed, likely due to electrostatic repulsion between the adjacent bilayers.</p></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":null,"pages":null},"PeriodicalIF":3.4,"publicationDate":"2024-01-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139414949","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural characterization of the antimicrobial peptides myxinidin and WMR in bacterial membrane mimetic micelles and bicelles","authors":"Yevhen K. Cherniavskyi ,&nbsp;Rosario Oliva ,&nbsp;Marco Stellato ,&nbsp;Pompea Del Vecchio ,&nbsp;Stefania Galdiero ,&nbsp;Annarita Falanga ,&nbsp;Sonja A. Dames ,&nbsp;D. Peter Tieleman","doi":"10.1016/j.bbamem.2024.184272","DOIUrl":"10.1016/j.bbamem.2024.184272","url":null,"abstract":"<div><p>Antimicrobial peptides<span><span><span> are a promising class of potential antibiotics that interact selectively with negatively charged lipid bilayers<span>. This paper presents the structural characterization of the antimicrobial peptides myxinidin and WMR associated with bacterial membrane mimetic </span></span>micelles<span><span> and bicelles by NMR, CD spectroscopy, and molecular dynamics simulations. Both peptides adopt a different conformation in the lipidic environment than in aqueous solution. The location of the peptides in micelles and bicelles has been studied by paramagnetic relaxation enhancement experiments with paramagnetic tagged 5- and 16-doxyl stearic acid (5-/16-SASL). Molecular dynamics simulations of multiple copies of the peptides were used to obtain an atomic level of detail on membrane-peptide and peptide-peptide interactions. Our results highlight an essential role of the negatively charged membrane mimetic in the structural stability of both myxinidin and WMR. The peptides localize predominantly in the membrane's headgroup region and have a noticeable membrane thinning effect on the overall </span>bilayer structure. Myxinidin and WMR show a different tendency to self-aggregate, which is also influenced by the membrane composition (DOPE/DOPG versus DOPE/DOPG/CL) and can be related to the previously observed difference in the ability of the peptides to disrupt different types of </span></span>model membranes.</span></p></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":null,"pages":null},"PeriodicalIF":3.4,"publicationDate":"2024-01-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139414972","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evidence for Ca2+-induced structural change in diluted GD3 ganglioside dispersions","authors":"Julia B. Ejarque ,&nbsp;Evandro L. Duarte ,&nbsp;M. Teresa Lamy ,&nbsp;Julio H.K. Rozenfeld","doi":"10.1016/j.bbamem.2024.184271","DOIUrl":"10.1016/j.bbamem.2024.184271","url":null,"abstract":"","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":null,"pages":null},"PeriodicalIF":3.4,"publicationDate":"2024-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139414906","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular dynamics simulations support a preference of cyclotide kalata B1 for phosphatidylethanolamine phospholipids","authors":"Ras Baizureen Roseli ,&nbsp;Yen-Hua Huang ,&nbsp;Sónia Troeira Henriques ,&nbsp;Quentin Kaas ,&nbsp;David J. Craik","doi":"10.1016/j.bbamem.2023.184268","DOIUrl":"10.1016/j.bbamem.2023.184268","url":null,"abstract":"<div><p>Kalata B1 (kB1), a naturally occurring cyclotide has been shown experimentally to bind lipid membranes that contain phosphatidylethanolamine (PE) phospholipids. Here, molecular dynamics simulations were used to explore its interaction with two phospholipids, palmitoyloleoylphosphatidylethanolamine (POPE), palmitoyloleoylphosphatidylcholine (POPC), and a heterogeneous membrane comprising POPC/POPE (90:10), to understand the basis for the selectivity of kB1 towards PE phospholipids. The simulations showed that in the presence of only 10 % POPE lipid, kB1 forms a stable binding complex with membrane bilayers. An ionic interaction between the E7 carboxylate group of kB1 and the ammonium group of PE headgroups consistently initiates binding of kB1 to the membrane. Additionally, stable noncovalent interactions such as hydrogen bonding (E7, T8, V10, G11, T13 and N15), cation–π (W23), and CH–π (W23) interactions between specific residues of kB1 and the lipid membrane play an important role in stabilizing the binding. These findings are consistent with a structure-activity relationship study on kB1 where lysine mutagenesis on the bioactive and hydrophobic faces of the peptide abolished membrane-dependent bioactivities. In summary, our simulations suggest the importance of residue E7 (in the bioactive face) in enabling kB1 to recognize and bind selectively to PE-containing phospholipids bilayers through ionic and hydrogen bonding interactions, and of W23 (in the hydrophobic face) for the association and insertion of kB1 into the lipid bilayer through cation–π and CH–π interactions. Overall, this work enhances our understanding of the molecular basis of the membrane binding and bioactivity of this prototypic cyclotide.</p></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":null,"pages":null},"PeriodicalIF":3.4,"publicationDate":"2024-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0005273623001505/pdfft?md5=900085e11db8861e250111cd44a5b7f3&pid=1-s2.0-S0005273623001505-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139374257","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"19F solid-state NMR approaches to probe antimicrobial peptide interactions with membranes in whole cells","authors":"Kiran Kumar ,&nbsp;Alexandre A. Arnold ,&nbsp;Raphaël Gauthier ,&nbsp;Marius Mamone ,&nbsp;Jean-François Paquin ,&nbsp;Dror E. Warschawski ,&nbsp;Isabelle Marcotte","doi":"10.1016/j.bbamem.2023.184269","DOIUrl":"10.1016/j.bbamem.2023.184269","url":null,"abstract":"<div><p><span><span>To address the global problem of bacterial antibiotic resistance, </span>antimicrobial peptides (AMPs) are considered promising therapeutic candidates due to their broad-spectrum and membrane-lytic activity. As preferential interactions with bacteria are crucial, it is equally important to investigate and understand their impact on eukaryotic cells. In this study, we employed </span>¹⁹<span>F solid-state nuclear magnetic resonance (ssNMR) as a novel approach to examine the interaction of AMPs with whole red blood cells (RBCs). We used RBC ghosts<span> (devoid of hemoglobin) and developed a protocol to label their lipid membranes<span> with palmitic acid (PA) monofluorinated at carbon positions 4, 8, or 14 on the acyl chain, allowing us to probe different locations in model and intact RBC ghost membranes. Our work revealed that changes in the </span></span></span>¹⁹F chemical shift anisotropy, monitored through a C<img>F bond order parameter (S_CF<span>), can provide insights into lipid bilayer dynamics. This information was also obtained using magic-angle spinning </span>¹⁹F ssNMR spectra with and without ¹H decoupling, by studying alterations in the second spectral moment (M₂) as well as the ¹⁹<span>F isotropic chemical shift, linewidth, T</span>₁, and T₂ relaxation times. The appearance of an additional isotropic peak with a smaller chemical shift anisotropy, a narrower linewidth, and a shorter T_1, induced by the AMP caerin 1.1, supports the presence of high-curvature regions in RBCs indicative of pore formation, analogous to its antimicrobial mechanism. In summary, the straightforward incorporation of monofluorinated FAs and rapid signal acquisition offer promising avenues for the study of whole cells using ¹⁹F ssNMR.</p></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":null,"pages":null},"PeriodicalIF":3.4,"publicationDate":"2024-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139097221","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural analysis of the NK-lysin-derived peptide NK-2 upon interaction with bacterial membrane mimetics consisting of phosphatidylethanolamine and phosphatidylglycerol","authors":"Jörg Andrä ,&nbsp;Christopher Aisenbrey ,&nbsp;U.S. Sudheendra ,&nbsp;Marc Prudhon ,&nbsp;Gerald Brezesinski ,&nbsp;Claudia Zschech ,&nbsp;Regine Willumeit-Römer ,&nbsp;Matthias Leippe ,&nbsp;Thomas Gutsmann ,&nbsp;Burkhard Bechinger","doi":"10.1016/j.bbamem.2023.184267","DOIUrl":"10.1016/j.bbamem.2023.184267","url":null,"abstract":"<div><p><span>NK-2 is an antimicrobial peptide<span><span><span><span> derived from helices 3 and 4 of the pore-forming protein of natural killer cells<span>, NK-lysin. It has potent activities against Gram-negative and Gram-positive bacteria, fungi and protozoan parasites without being toxic to healthy human cells. In biophysical assays its membrane activities were found to require phosphatidylglycerol (PG) and </span></span>phosphatidylethanolamine (PE), </span>lipids<span> which dominate the composition of bacterial membranes. Here the structure and activities of NK-2 in binary mixtures of different PE/PG composition were investigated. CD spectroscopy reveals that a threshold concentration of 50 % PG is needed for efficient membrane association of NK-2 concomitant with a random coil – helix transition. Association with PE occurs but is qualitatively different when compared to PG membranes. Oriented solid-state </span></span>NMR spectroscopy of NK-2 specifically labelled with </span></span>¹⁵<span>N indicates that the NK-2 helices are oriented parallel to the PG bilayer surface. Upon reduction of the PG content to 20 mol% interactions are weaker and/or an in average more tilted orientation is observed. Fluorescence spectroscopy of differently labelled lipids is in agreement of an interfacial localisation of both helices where the C-terminal end is in a less hydrophobic environment. By inserting into the membrane interface and interacting differently with PE and PG the peptides probably induce high curvature strain which result in membrane openings and rupture.</span></p></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":null,"pages":null},"PeriodicalIF":3.4,"publicationDate":"2023-12-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139062518","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}