{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T23:26:53Z","timestamp":1788564413944,"version":"build-2803163510"},"reference-count":74,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2025,11,27]],"date-time":"2025-11-27T00:00:00Z","timestamp":1764201600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["24-25-00160"],"award-info":[{"award-number":["24-25-00160"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceutics"],"abstract":"<jats:p>Background\/Objectives: Methicillin-resistant Staphylococcus aureus (MRSA) poses a significant global health threat due to its increasing resistance to conventional antibiotics. Antimicrobial peptides (AMPs) derived from natural sources represent a promising alternative. Fragments of spider membrane-active toxins can serve as AMPs with anti-MRSA activity. Methods: To demonstrate this, amino acid sequences of approximately 2000 linear spider venom peptides were fragmented into 9\u201322-residue-long moieties (75,235 in total) and pre-trained neural networks were used to predict their anti-MRSA activity. As many as 15 peptides with high predicted activity were synthesized, and three AMPs with high anti-MRSA and low hemolytic activities were selected. One of these peptides was studied using high-resolution 1H-, 13C-, and 15N-NMR spectroscopy in an aqueous solution and lyso-palmitoylphosphatidylglycerol (LPPG) micelles. Wide-line 31P-NMR was applied to multilamellar phospholipid liposomes composed of phosphatidylcholine (PC) or phosphatidylglycerol (PG). Results: Low hemolytic activity is explained by non-specific interaction with PC whereas high antibacterial activity arises from specific interaction with PG accompanied with the formation of a tight complex between the N-terminal tripeptide fragment and PG headgroup. The structure of a such complex, stabilized by an ionic interaction between the N-terminal NH3+ group and the lipid phosphate, was determined based on peptide\u2013LPPG NOEs. The most favorable ratio between anti-MRSA and hemolytic activities, i.e., selectivity of the peptides, is attained when the tripeptide consists exclusively of phenylalanine and tryptophan residues. Confocal microscopy confirmed that the most selective peptide deteriorates the plasma membrane of S. aureus. Conclusions: This approach may enable the production of highly selective AMPs against Stapylococci, including MRSA.<\/jats:p>","DOI":"10.3390\/pharmaceutics17121526","type":"journal-article","created":{"date-parts":[[2025,11,27]],"date-time":"2025-11-27T10:25:16Z","timestamp":1764239116000},"page":"1526","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["NMR Unveils Activity Mechanism of Linear Spider Venom Peptide Fragments Selected by Neural Networks Against Staphylococci Including MRSA"],"prefix":"10.3390","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7884-3257","authenticated-orcid":false,"given":"Pavel A.","family":"Mironov","sequence":"first","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16\/10 Miklukho-Maklaya str., Moscow 117997, Russia"},{"name":"Bioengineering Department, Faculty of Biology, Lomonosov Moscow State University, 1 Leninsky Gory str., Moscow 119234, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna A.","family":"Baranova","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16\/10 Miklukho-Maklaya str., Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8961-5890","authenticated-orcid":false,"given":"Vera A.","family":"Alferova","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16\/10 Miklukho-Maklaya str., Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalya S.","family":"Egorova","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16\/10 Miklukho-Maklaya str., Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5217-3937","authenticated-orcid":false,"given":"Anastasia A.","family":"Ignatova","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16\/10 Miklukho-Maklaya str., Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1596-9506","authenticated-orcid":false,"given":"Alexey V.","family":"Feofanov","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16\/10 Miklukho-Maklaya str., Moscow 117997, Russia"},{"name":"Bioengineering Department, Faculty of Biology, Lomonosov Moscow State University, 1 Leninsky Gory str., Moscow 119234, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1383-3522","authenticated-orcid":false,"given":"Zakhar O.","family":"Shenkarev","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16\/10 Miklukho-Maklaya str., Moscow 117997, Russia"},{"name":"Moscow Center for Advanced Studies, 20 Kulakova str., Moscow 123592, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2289-6023","authenticated-orcid":false,"given":"Peter V.","family":"Dubovskii","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16\/10 Miklukho-Maklaya str., Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,11,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1038\/s41579-024-01054-w","article-title":"ESKAPE Pathogens: Antimicrobial Resistance, Epidemiology, Clinical Impact and Therapeutics","volume":"22","author":"Miller","year":"2024","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"e216","DOI":"10.1016\/S1473-3099(20)30327-3","article-title":"The Value of Antimicrobial Peptides in the Age of Resistance","volume":"20","author":"Magana","year":"2020","journal-title":"Lancet Infect. Dis."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1016\/j.bbamem.2019.07.012","article-title":"Modulation of Antimicrobial Potency of Human Cathelicidin Peptides against the ESKAPE Pathogens and In Vivo Efficacy in a Murine Catheter-Associated Biofilm Model","volume":"1861","author":"Narayana","year":"2019","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2215","DOI":"10.1021\/acsinfecdis.3c00293","article-title":"Enhanced Antimicrobial Screening Sensitivity Enabled the Identification of an Ultrashort Peptide KR-8 for Engineering of LL-37mini to Combat Drug-Resistant Pathogens","volume":"9","author":"Mechesso","year":"2023","journal-title":"ACS Infect. Dis."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1021\/cb500475y","article-title":"Transformation of Human Cathelicidin LL-37 into Selective, Stable, and Potent Antimicrobial Compounds","volume":"9","author":"Wang","year":"2014","journal-title":"ACS Chem. Biol."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Mirzaei, R., Esmaeili Gouvarchin Ghaleh, H., and Ranjbar, R. (2023). Antibiofilm Effect of Melittin Alone and in Combination with Conventional Antibiotics toward Strong Biofilm of MDR-MRSA and -Pseudomonas aeruginosa. Front. Microbiol., 14.","DOI":"10.3389\/fmicb.2023.1030401"},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Chen, S., Zhang, P., Xiao, L., Liu, Y., Wu, K., Ni, G., Li, H., Wang, T., Wu, X., and Chen, G. (2021). Caerin 1.1 and 1.9 Peptides from Australian Tree Frog Inhibit Antibiotic-Resistant Bacteria Growth in a Murine Skin Infection Model. Microbiol. Spectr., 9.","DOI":"10.1128\/Spectrum.00051-21"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.micpath.2018.04.008","article-title":"Venom-Derived Peptide Mastoparan-1 Eradicates Planktonic and Biofilm-Embedded Methicillin-Resistant Staphylococcus aureus Isolates","volume":"119","author":"Memariani","year":"2018","journal-title":"Microb. Pathog."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Kuhn-Nentwig, L., Lischer, H.E.L., Pek\u00e1r, S., Langenegger, N., Albo, M.J., Isaia, M., and Nentwig, W. (2021). Linear Peptides-A Combinatorial Innovation in the Venom of Some Modern Spiders. Front. Mol. Biosci., 8.","DOI":"10.3389\/fmolb.2021.705141"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1007\/s00726-009-0385-x","article-title":"LyeTx I, a Potent Antimicrobial Peptide from the Venom of the Spider Lycosa erythrognatha","volume":"39","author":"Santos","year":"2010","journal-title":"Amino Acids"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"20983","DOI":"10.1074\/jbc.M602168200","article-title":"Latarcins, Antimicrobial and Cytolytic Peptides from the Venom of the Spider Lachesana tarabaevi (Zodariidae) That Exemplify Biomolecular Diversity","volume":"281","author":"Kozlov","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"4501","DOI":"10.1007\/s00018-015-2016-x","article-title":"Latarcins: Versatile Spider Venom Peptides","volume":"72","author":"Dubovskii","year":"2015","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Wadhwani, P., Sekaran, S., Strandberg, E., B\u00fcrck, J., Chugh, A., and Ulrich, A.S. (2021). Membrane Interactions of Latarcins: Antimicrobial Peptides from Spider Venom. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms221810156"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1134\/S1068162007040024","article-title":"Synthetic analogues of antimicrobial peptides from the venom of the Central Asian spider Lachesana tarabaevi","volume":"33","author":"Vassilevskii","year":"2007","journal-title":"Russ. J. Bioorg. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"3525","DOI":"10.1021\/bi702203w","article-title":"Three-Dimensional Structure\/Hydrophobicity of Latarcins Specifies Their Mode of Membrane Activity","volume":"47","author":"Dubovskii","year":"2008","journal-title":"Biochemistry"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate Structure Prediction of Biomolecular Interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"D1087","DOI":"10.1093\/nar\/gkv1278","article-title":"APD3: The Antimicrobial Peptide Database as a Tool for Research and Education","volume":"44","author":"Wang","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"D288","DOI":"10.1093\/nar\/gkaa991","article-title":"DBAASP v3: Database of Antimicrobial\/Cytotoxic Activity and Structure of Peptides as a Resource for Development of New Therapeutics","volume":"49","author":"Pirtskhalava","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"D488","DOI":"10.1093\/nar\/gkab651","article-title":"DRAMP 3.0: An Enhanced Comprehensive Data Repository of Antimicrobial Peptides","volume":"50","author":"Shi","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1007\/s00249-012-0867-8","article-title":"Unusual Titration of the Membrane-Bound Artificial Hemagglutinin Fusion Peptide","volume":"41","author":"Dubovskii","year":"2012","journal-title":"Eur. Biophys. J."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1007\/978-1-4939-2239-0_2","article-title":"Protein Structural Information Derived from NMR Chemical Shift with the Neural Network Program TALOS-N","volume":"1260","author":"Shen","year":"2015","journal-title":"Methods Mol. Biol."},{"key":"ref_22","first-page":"353","article-title":"Automated NMR Structure Calculation with CYANA","volume":"278","year":"2004","journal-title":"Methods Mol. Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"2038","DOI":"10.1046\/j.1432-1033.2003.03580.x","article-title":"Interaction of the P-Type Cardiotoxin with Phospholipid Membranes","volume":"270","author":"Dubovskii","year":"2003","journal-title":"Eur. J. Biochem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/j.ssnmr.2005.10.009","article-title":"Modeling of 31P-NMR Spectra of Magnetically Oriented Phospholipid Liposomes: A New Analytical Solution","volume":"29","author":"Dubinnyi","year":"2006","journal-title":"Solid State Nucl. Magn. Reson."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.jmr.2007.12.001","article-title":"PGSTE-WATERGATE: An STE-Based PGSE NMR Sequence with Excellent Solvent Suppression","volume":"191","author":"Zheng","year":"2008","journal-title":"J. Magn. Reson."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1023\/B:JNMR.0000032560.43738.6a","article-title":"Characterization of Phospholipid Mixed Micelles by Translational Diffusion","volume":"29","author":"Chou","year":"2004","journal-title":"J. Biomol. NMR"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"R16","DOI":"10.1103\/PhysRevE.50.R16","article-title":"Dynamics of Hard-Sphere Suspensions","volume":"50","author":"Tokuyama","year":"1994","journal-title":"Phys. Rev. E"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2309","DOI":"10.4155\/fmc-2018-0170","article-title":"Improving Therapeutic Potential of Antibacterial Spider Venom Peptides: Coarse-Grain Molecular Dynamics Guided Approach","volume":"10","author":"Dubovskii","year":"2018","journal-title":"Future Med. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Du, Z., Ding, X., Xu, Y., and Li, Y. (2023). UniDL4BioPep: A Universal Deep Learning Architecture for Binary Classification in Peptide Bioactivity. Brief. Bioinform., 24.","DOI":"10.1093\/bib\/bbad135"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Lee, B., Shin, M.K., Yoo, J.S., Jang, W., and Sung, J.-S. (2022). Identifying Novel Antimicrobial Peptides from Venom Gland of Spider Pardosa astrigera by Deep Multi-Task Learning. Front. Microbiol., 13.","DOI":"10.3389\/fmicb.2022.971503"},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Li, C., Sutherland, D., Hammond, S.A., Yang, C., Taho, F., Bergman, L., Houston, S., Warren, R.L., Wong, T., and Hoang, L.M.N. (2022). AMPlify: Attentive Deep Learning Model for Discovery of Novel Antimicrobial Peptides Effective against WHO Priority Pathogens. BMC Genom., 23.","DOI":"10.1186\/s12864-022-08310-4"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Li, C., Warren, R.L., and Birol, I. (2023). Models and Data of AMPlify: A Deep Learning Tool for Antimicrobial Peptide Prediction. BMC Res. Notes, 16.","DOI":"10.1186\/s13104-023-06279-1"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1126\/science.adn1369","article-title":"Two Codependent Routes Lead to High-Level MRSA","volume":"386","author":"Wacnik","year":"2024","journal-title":"Science"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"32653","DOI":"10.1021\/acsomega.2c04305","article-title":"SCMRSA: A New Approach for Identifying and Analyzing Anti-MRSA Peptides Using Estimated Propensity Scores of Dipeptides","volume":"7","author":"Charoenkwan","year":"2022","journal-title":"ACS Omega"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.mencom.2015.01.026","article-title":"Cobra Cytotoxins: Determinants of Antibacterial Activity","volume":"25","author":"Dubovskii","year":"2015","journal-title":"Mendeleev Commun."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1002\/bip.20911","article-title":"Effects of Net Charge and the Number of Positively Charged Residues on the Biological Activity of Amphipathic Alpha-Helical Cationic Antimicrobial Peptides","volume":"90","author":"Jiang","year":"2008","journal-title":"Biopolymers"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","article-title":"A Simple Method for Displaying the Hydropathic Character of a Protein","volume":"157","author":"Kyte","year":"1982","journal-title":"J. Mol. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"de Souza, A.N., Cardoso, G.d.A., Nunes, L.O., Aisenbrey, C., Salnikov, E., de Souza, K.R., Saad, A., de Lima, M.E., Resende, J.M., and Bechinger, B. (2025). Comparative Structural and Biophysical Investigation of Lycosa erythrognatha Toxin I (LyeTx I) and Its Analog LyeTx I-b. Antibiotics, 14.","DOI":"10.3390\/antibiotics14010066"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Reis, P.V.M., Boff, D., Verly, R.M., Melo-Braga, M.N., Cort\u00e9s, M.E., Santos, D.M., Pimenta, A.M.d.C., Amaral, F.A., Resende, J.M., and de Lima, M.E. (2018). LyeTxI-b, a Synthetic Peptide Derived From Lycosa erythrognatha Spider Venom, Shows Potent Antibiotic Activity in Vitro and in Vivo. Front. Microbiol., 9.","DOI":"10.3389\/fmicb.2018.00667"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1002\/mrc.1132","article-title":"Translational Diffusion Measured by PFG-NMR on Full Length and Fragments of the Alzheimer A\u03b2(1\u201340) Peptide. Determination of Hydrodynamic Radii of Random Coil Peptides of Varying Length","volume":"40","author":"Danielsson","year":"2002","journal-title":"Magn. Reson. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1006\/jmre.2000.2170","article-title":"HYDRONMR: Prediction of NMR Relaxation of Globular Proteins from Atomic-Level Structures and Hydrodynamic Calculations","volume":"147","author":"Huertas","year":"2000","journal-title":"J. Magn. Reson."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1006\/jmbi.1993.1631","article-title":"Local Conformations of Peptides Representing the Entire Sequence of Bovine Pancreatic Trypsin Inhibitor and Their Roles in Folding","volume":"234","author":"Kemmink","year":"1993","journal-title":"J. Mol. Biol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1006\/jmbi.1993.1144","article-title":"Local Structure Due to an Aromatic-Amide Interaction Observed by 1H-Nuclear Magnetic Resonance Spectroscopy in Peptides Related to the N Terminus of Bovine Pancreatic Trypsin Inhibitor","volume":"230","author":"Kemmink","year":"1993","journal-title":"J. Mol. Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1007\/s10858-014-9862-y","article-title":"pH-Dependent Random Coil (1)H, (13)C, and (15)N Chemical Shifts of the Ionizable Amino Acids: A Guide for Protein pKa Measurements","volume":"60","author":"Platzer","year":"2014","journal-title":"J. Biomol. NMR"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"14346","DOI":"10.1021\/ja8062327","article-title":"Bacterial Membranes as Predictors of Antimicrobial Potency","volume":"130","author":"Epand","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"12427","DOI":"10.1021\/jp073016l","article-title":"Size and Shape of Detergent Micelles Determined by Small-Angle X-Ray Scattering","volume":"111","author":"Lipfert","year":"2007","journal-title":"J. Phys. Chem. B"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1093\/bioinformatics\/btp111","article-title":"PLATINUM: A Web Tool for Analysis of Hydrophobic\/Hydrophilic Organization of Biomolecular Complexes","volume":"25","author":"Pyrkov","year":"2009","journal-title":"Bioinformatics"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/S0001-8686(00)00056-7","article-title":"Phase Diagrams of Systems with Cationic Alpha-Helical Membrane-Spanning Model Peptides and Dioleoylphosphatidylcholine","volume":"89\u201390","author":"Strandberg","year":"2001","journal-title":"Adv. Colloid Interface Sci."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2451","DOI":"10.1021\/bi00175a013","article-title":"Lipid Specificity in the Interaction of Cytochrome c with Anionic Phospholipid Bilayers Revealed by Solid-State 31P NMR","volume":"33","author":"Pinheiro","year":"1994","journal-title":"Biochemistry"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"7127","DOI":"10.1021\/jp070066h","article-title":"Opposing Effects of Cation Binding and Hydration on the Bending Rigidity of Anionic Lipid Bilayers","volume":"111","author":"Claessens","year":"2007","journal-title":"J. Phys. Chem. B"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/0005-2736(80)90391-0","article-title":"Effects of Tumbling and Lateral Diffusion on Phosphatidylcholine Model Membrane 31P-NMR Lineshapes","volume":"603","author":"Burnell","year":"1980","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/0005-2736(82)90092-X","article-title":"Effect of Glycophorin on Lipid Polymorphism. A 31P-NMR Study","volume":"685","author":"Taraschi","year":"1982","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"7101","DOI":"10.1021\/bi00346a013","article-title":"Penetration of a Cardiotoxin into Cardiolipin Model Membranes and Its Implications on Lipid Organization","volume":"24","author":"Batenburg","year":"1985","journal-title":"Biochemistry"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"10759","DOI":"10.1021\/bi060635w","article-title":"Spatial Structure and Activity Mechanism of a Novel Spider Antimicrobial Peptide","volume":"45","author":"Dubovskii","year":"2006","journal-title":"Biochemistry"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1002\/jms.577","article-title":"De Novo Sequencing of Antimicrobial Peptides Isolated from the Venom Glands of the Wolf Spider Lycosa singoriensis","volume":"39","author":"Budnik","year":"2004","journal-title":"J. Mass Spectrom."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Oh, J.H., Park, J., and Park, Y. (2022). Anti-Biofilm and Anti-Inflammatory Effects of Lycosin-II Isolated from Spiders against Multi-Drug Resistant Bacteria. Biochim. Biophys. Acta Biomembr., 1864.","DOI":"10.1016\/j.bbamem.2021.183769"},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Park, J., Kim, H., Kang, H.-K., Choi, M.-C., and Park, Y. (2022). Lycosin-II Exhibits Antifungal Activity and Inhibits Dual-Species Biofilm by Candida albicans and Staphylococcus aureus. J. Fungi, 8.","DOI":"10.3390\/jof8090901"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Tan, H., Wang, J., Song, Y., Liu, S., Lu, Z., Luo, H., and Tang, X. (2022). Antibacterial Potential Analysis of Novel \u03b1-Helix Peptides in the Chinese Wolf Spider Lycosa sinensis. Pharmaceutics, 14.","DOI":"10.3390\/pharmaceutics14112540"},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Wang, K., Mwangi, J., Cao, K., Wang, Y., Gao, J., Yang, M., Michira, B.B., Lu, Q., and Li, J. (2024). Peptide Toxin Diversity and a Novel Antimicrobial Peptide from the Spider Oxyopes forcipiformis. Toxins, 16.","DOI":"10.3390\/toxins16110466"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Oh, J.W., Shin, M.K., Park, H.-R., Kim, S., Lee, B., Yoo, J.S., Chi, W.-J., and Sung, J.-S. (2024). PA-Win2: In Silico-Based Discovery of a Novel Peptide with Dual Antibacterial and Anti-Biofilm Activity. Antibiotics, 13.","DOI":"10.3390\/antibiotics13121113"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"107657","DOI":"10.1016\/j.toxicon.2024.107657","article-title":"Characterization of an Antimicrobial Peptide Family from the Venom Gland of Heteropoda venatoria","volume":"241","author":"Peng","year":"2024","journal-title":"Toxicon"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1177\/1535370220966963","article-title":"Shortened Derivatives from Native Antimicrobial Peptide LyeTx I: In Vitro and In Vivo Biological Activity Assessment","volume":"246","author":"Fuscaldi","year":"2021","journal-title":"Exp. Biol. Med."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Vieira, A.P.G.C., de Souza, A.N., Lima, W.G., Brito, J.C.M., Simi\u00e3o, D.C., Gon\u00e7alves, L.V.R., Cordeiro, L.P.B., de Oliveira Scoaris, D., Fernandes, S.O.A., and Resende, J.M. (2024). The Synthetic Peptide LyeTx I mn\u2206K, Derived from Lycosa erythrognatha Spider Toxin, Is Active against Methicillin-Resistant Staphylococcus aureus (MRSA) In Vitro and In Vivo. Antibiotics, 13.","DOI":"10.3390\/antibiotics13030248"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"e0042424","DOI":"10.1128\/aac.00424-24","article-title":"LC-AMP-I1, a Novel Venom-Derived Antimicrobial Peptide from the Wolf Spider Lycosa coelestis","volume":"69","author":"Wang","year":"2025","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1007\/BF00277157","article-title":"Lipoteichoic Acid and Lipids in the Membrane of Staphylococcus aureus","volume":"183","author":"Fischer","year":"1994","journal-title":"Med. Microbiol. Immunol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"3271","DOI":"10.1016\/j.bbamem.2007.08.005","article-title":"Determination of Solution Structure and Lipid Micelle Location of an Engineered Membrane Peptide by Using One NMR Experiment and One Sample","volume":"1768","author":"Wang","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/j.chembiol.2004.04.020","article-title":"Structural Transitions as Determinants of the Action of the Calcium-Dependent Antibiotic Daptomycin","volume":"11","author":"Jung","year":"2004","journal-title":"Chem. Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1038\/s41467-020-15257-1","article-title":"Ca2+-Daptomycin Targets Cell Wall Biosynthesis by Forming a Tripartite Complex with Undecaprenyl-Coupled Intermediates and Membrane Lipids","volume":"11","author":"Grein","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"18694","DOI":"10.1002\/anie.202104528","article-title":"Gausemycins\u2005A,B: Cyclic Lipoglycopeptides from Streptomyces sp.","volume":"60","author":"Tyurin","year":"2021","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1021\/acs.jnatprod.3c00612","article-title":"Gausemycin Antibiotic Family Acts via Ca2+-Dependent Membrane Targeting","volume":"87","author":"Kravchenko","year":"2024","journal-title":"J. Nat. Prod."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Pereira-Dias, L., Oliveira-Pinto, P.R., Fernandes, J.O., Regalado, L., Mendes, R., Teixeira, C., Mariz-Ponte, N., Gomes, P., and Santos, C. (2023). Peptaibiotics: Harnessing the Potential of Microbial Secondary Metabolites for Mitigation of Plant Pathogens. Biotechnol. Adv., 68.","DOI":"10.1016\/j.biotechadv.2023.108223"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1016\/S0006-3495(02)75438-6","article-title":"Spatial Structure of Zervamicin IIB Bound to DPC Micelles: Implications for Voltage-Gating","volume":"82","author":"Shenkarev","year":"2002","journal-title":"Biophys. J."},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Dalla Torre, C., Sannio, F., Battistella, M., Docquier, J.-D., and De Zotti, M. (2023). Peptaibol Analogs Show Potent Antibacterial Activity against Multidrug Resistant Opportunistic Pathogens. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24097997"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"68","DOI":"10.32607\/20758251-2011-3-2-68-78","article-title":"N-Terminal Moiety of Antimicrobial Peptide Ltc1-k Increases Its Toxicity for Eukaryotic Cells","volume":"3","author":"Samsonova","year":"2011","journal-title":"Acta Naturae"}],"container-title":["Pharmaceutics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4923\/17\/12\/1526\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,11,27]],"date-time":"2025-11-27T10:33:44Z","timestamp":1764239624000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4923\/17\/12\/1526"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11,27]]},"references-count":74,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["pharmaceutics17121526"],"URL":"https:\/\/doi.org\/10.3390\/pharmaceutics17121526","relation":{},"ISSN":["1999-4923"],"issn-type":[{"value":"1999-4923","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,11,27]]}}}