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Antimicrobial peptides (AMPs) are promising candidates because of their broad-spectrum activity. In this study, we designed three derivatives (i.e., Analog-1, -2, and -3) of the native peptide, Wuchuanin-A1, for improving their antibacterial activity against Staphylococcus aureus and Escherichia coli. The hypothesis is that the antibacterial activity of these peptides can be improved by increasing their amphipathicity (evaluated using hydrophobic moment analysis), \u03b1-helical stability, and membrane binding properties. In this case, the residues of native peptide were mutated to form an amphipathic peptide, referred to here as Analog-1. Then, the N- and C-termini of Analog-1 were capped with acetyl and amide groups, respectively, to produce Analog-2. Finally, the Asp and Arg residues in Analog-2 were mutated to Glu and Lys residues, respectively, in Analog-3. Circular dichroism (CD) spectra in trifluoroethanol (TFE) or methanol (MeOH) showed that Analog-3 has the highest \u03b1-helical stability, followed by Analog-2 and Analog-1. Two-dimensional nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics (MD) simulations studies indicated that Analog-2 and -3 have a stable continuous \u03b1-helical structure. Both Analog-2 and -3 can form dimer or oligomer at higher concentrations. All three analogs can bind to model membranes of Gram-positive and Gram-negative bacteria, with Analog-3 as the best membrane binding affinity through Langmuir monolayer analysis. Both Analog-2 and -3 have better antibacterial activities against S. aureus and E. coli compared to Analog-1 and the native peptide, with minimum inhibitory concentration (MIC) values 3.91 \u00b5g\/mL against S. aureus and 62.5 \u00b5g\/mL against E. coli, which are 2\u201332-fold lower than those of Analog-1. In addition, Analog-2 and -3 have better activity against S. aureus than E. coli bacteria. We proposed that the increase in antibacterial activity of Analog-2 and -3 was due to the \u03b1-helical stability, amphipathic structure, and membrane binding properties.<\/jats:p>","DOI":"10.3390\/life15101568","type":"journal-article","created":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T12:04:52Z","timestamp":1759925092000},"page":"1568","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Design, Structural Stability, Membrane Binding, and Antibacterial Activity of Novel Antimicrobial Peptides Derived from Wuchuanin-A1"],"prefix":"10.3390","volume":"15","author":[{"given":"Rizki A.","family":"Putri","sequence":"first","affiliation":[{"name":"Department of Chemistry, Faculty of Mathematics and Natural Sciences, Universitas Gadjah Mada, Sekip Utara, Yogyakarta 55281, Indonesia"},{"name":"Department of Pharmaceutical Chemistry, School of Pharmacy, The University of Kansas, Simons Laboratories, 2095 Constant Ave., Lawrence, KS 66045, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahmad","family":"Habibie","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Mathematics and Natural Sciences, Universitas Gadjah Mada, Sekip Utara, Yogyakarta 55281, Indonesia"},{"name":"Department of Pharmaceutical Chemistry, School of Pharmacy, The University of Kansas, Simons Laboratories, 2095 Constant Ave., Lawrence, KS 66045, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5821-5253","authenticated-orcid":false,"given":"Prajnaparamita","family":"Dhar","sequence":"additional","affiliation":[{"name":"Department of Chemical and Petroleum Engineering, School of Engineering, The University of Kansas, Eaton Hall, 1520 W 15th St, Lawrence, KS 66045, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2358-1349","authenticated-orcid":false,"given":"Krzysztof","family":"Kuczera","sequence":"additional","affiliation":[{"name":"Department of Chemistry, College of Liberal Arts & Sciences, The University of Kansas, Gray-Little Hall, 1567 Irving Hill Rd, Lawrence, KS 66045, USA"},{"name":"Department of Molecular Biosciences, College of Liberal Arts & Sciences, The University of Kansas, Haworth Hall, 1200 Sunnyside Avenue, Lawrence, KS 66045, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Respati Tri","family":"Swasono","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Mathematics and Natural Sciences, Universitas Gadjah Mada, Sekip Utara, Yogyakarta 55281, Indonesia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7764-9778","authenticated-orcid":false,"given":"Muhammad Saifur","family":"Rohman","sequence":"additional","affiliation":[{"name":"Department of Agricultural Microbiology, Universitas Gadjah Mada, Jl Flora, Kompleks Bulaksumur, UGM, Yogyakarta 55281, Indonesia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0615-5241","authenticated-orcid":false,"given":"Tri Joko","family":"Raharjo","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Mathematics and Natural Sciences, Universitas Gadjah Mada, Sekip Utara, Yogyakarta 55281, Indonesia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7250-0627","authenticated-orcid":false,"given":"Teruna J.","family":"Siahaan","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, School of Pharmacy, The University of Kansas, Simons Laboratories, 2095 Constant Ave., Lawrence, KS 66045, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,10,8]]},"reference":[{"key":"ref_1","unstructured":"O\u2019Neill, J. (2014). Antimicrobial Resistance: Tackling a Crisis for the Health and Wealth of Nations, Review on Antimicrobial Resistance."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"100954","DOI":"10.1016\/j.drup.2023.100954","article-title":"Antimicrobial peptides for combating drug-resistant bacterial infections","volume":"68","author":"Xuan","year":"2023","journal-title":"Drug Resist. Updates"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Preusske, N., Sonnichsen, F.D., and Leippe, M. (2023). A guided tour through alpha-helical peptide antibiotics and their targets. Biosci. Rep., 43.","DOI":"10.1042\/BSR20230474"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2062","DOI":"10.1021\/acsinfecdis.3c00189","article-title":"Small-Molecule Antibiotic Drug Development: Need and Challenges","volume":"9","author":"Bergkessel","year":"2023","journal-title":"ACS Infect. Dis."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/0922-4106(92)90045-W","article-title":"Magainin 2, a natural antibiotic from frog skin, forms ion channels in lipid bilayer membranes","volume":"226","author":"Cruciani","year":"1992","journal-title":"Eur. J. Pharmacol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1023\/A:1018698002314","article-title":"Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol\/water solution","volume":"9","author":"Gesell","year":"1997","journal-title":"J. Biomol. NMR"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1016\/j.bbamem.2008.10.009","article-title":"Structure, membrane orientation, mechanism, and function of pexiganan\u2014A highly potent antimicrobial peptide designed from magainin","volume":"1788","author":"Gottler","year":"2009","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1529\/biophysj.105.073890","article-title":"Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin","volume":"91","author":"Ramamoorthy","year":"2006","journal-title":"Biophys. J."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2196","DOI":"10.1021\/acs.accounts.1c00047","article-title":"Advances in Molecular Understanding of alpha-Helical Membrane-Active Peptides","volume":"54","author":"Kabelka","year":"2021","journal-title":"Acc. Chem. Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1007\/s13238-014-0061-0","article-title":"Role of helicity of \u03b1-helical antimicrobial peptides to improve specificity","volume":"5","author":"Huang","year":"2014","journal-title":"Protein Cell"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"5757","DOI":"10.1529\/biophysj.108.133488","article-title":"Magainin 2 in action: Distinct modes of membrane permeabilization in living bacterial and mammalian cells","volume":"95","author":"Imura","year":"2008","journal-title":"Biophys. J."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2195","DOI":"10.1128\/IAI.01414-13","article-title":"Hydrophobic determinants of alpha-defensin bactericidal activity","volume":"82","author":"Tai","year":"2014","journal-title":"Infect. Immun."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1021\/pr200782u","article-title":"Extremely abundant antimicrobial peptides existed in the skins of nine kinds of Chinese odorous frogs","volume":"11","author":"Yang","year":"2012","journal-title":"J. Proteome Res."},{"key":"ref_14","first-page":"100182","article-title":"Effect of charge on the antimicrobial activity of alpha-helical amphibian antimicrobial peptide","volume":"4","author":"Islam","year":"2023","journal-title":"Curr. Res. Microb. Sci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2652","DOI":"10.1021\/acs.jpcb.3c07511","article-title":"Estimation of Peptide Helicity from Circular Dichroism Using the Ensemble Model","volume":"128","author":"Zavrtanik","year":"2024","journal-title":"J. Phys. Chem. B"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1021\/bi982271g","article-title":"Fragment reconstitution of a small protein: Folding energetics of the reconstituted immunoglobulin binding domain B1 of streptococcal protein G","volume":"38","author":"Honda","year":"1999","journal-title":"Biochemistry"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Stephanie, F., Tambunan, U.S.F., Kuczera, K., and Siahaan, T.J. (2024). Structure of a Cyclic Peptide as an Inhibitor of Mycobacterium tuberculosis Transcription: NMR and Molecular Dynamics Simulations. Pharmaceuticals, 17.","DOI":"10.3390\/ph17111545"},{"key":"ref_18","unstructured":"Wuthrich, K. (1991). NMR of Proteins and Nucleic Acids, Wiley-Interscience."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1110\/ps.0240103","article-title":"The role of \u03b1-, 310-, and \u03c0-helix in helix\u2192coil transitions","volume":"12","author":"Armen","year":"2003","journal-title":"Protein Sci."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1007\/BF00228148","article-title":"AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR","volume":"8","author":"Laskowski","year":"1996","journal-title":"J. Biomol. NMR"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"W41","DOI":"10.1093\/nar\/gkaa362","article-title":"ARIAweb: A server for automated NMR structure calculation","volume":"48","author":"Allain","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1002\/jcc.20945","article-title":"CHARMM-GUI: A web-based graphical user interface for CHARMM","volume":"29","author":"Jo","year":"2008","journal-title":"J. Comp. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1021\/acs.jctc.5b00935","article-title":"CHARMM-GUI Input Generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM\/OpenMM Simulations Using the CHARMM36 Additive Force Field","volume":"12","author":"Lee","year":"2016","journal-title":"J. Chem. Theory Comput."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of Simple Potential Functions for Simulating Liquid Water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J. Chem. Phys."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers","volume":"1","author":"Abraham","year":"2015","journal-title":"SoftwareX"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/nmeth.4067","article-title":"CHARMM36m: An improved force field for folded and intrinsically disordered proteins","volume":"14","author":"Huang","year":"2017","journal-title":"Nat. Methods"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"014101","DOI":"10.1063\/1.2408420","article-title":"Canonical sampling through velocity rescaling","volume":"126","author":"Bussi","year":"2007","journal-title":"J. Chem. Phys."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"R55","DOI":"10.1016\/S0969-2126(99)80033-1","article-title":"New tricks for modelers from the crystallography toolkit: The particle mesh Ewald algorithm and its use in nucleic acid simulations","volume":"7","author":"Darden","year":"1999","journal-title":"Structure"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1021\/ct700200b","article-title":"P-LINCS: A Parallel Linear Constraint Solver for Molecular Simulation","volume":"4","author":"Hess","year":"2008","journal-title":"J. Chem. Theory Comput."},{"key":"ref_30","unstructured":"(PyMOL 3.1, 2024). PyMOL 3.1, The PyMOL Molecular Graphics System."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Pinto, O.A., and Disalvo, E.A. (2019). A new model for lipid monolayer and bilayers based on thermodynamics of irreversible processes. PLoS ONE, 14.","DOI":"10.1371\/journal.pone.0212269"},{"key":"ref_32","unstructured":"(2020). Methods for Antimicrobial Broth Dilution and Disk Diffusion Susceptibility Testing of Bacteria Isolated from Aquatic Animals (Standard No. VET03)."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/cimb44010001","article-title":"Structural and Functional Characterization of a Novel Recombinant Antimicrobial Peptide from Hermetia illucens","volume":"44","author":"Moretta","year":"2021","journal-title":"Curr. Issues Mol. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2876","DOI":"10.1038\/nprot.2006.202","article-title":"Using circular dichroism spectra to estimate protein secondary structure","volume":"1","author":"Greenfield","year":"2006","journal-title":"Nat. Protoc."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1007\/978-1-0716-0892-0_11","article-title":"BeStSel: From Secondary Structure Analysis to Protein Fold Prediction by Circular Dichroism Spectroscopy","volume":"2199","author":"Micsonai","year":"2021","journal-title":"Methods Mol. Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"31995","DOI":"10.1074\/jbc.M114.583369","article-title":"A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties","volume":"289","author":"Battaglia","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"2981","DOI":"10.1140\/epjs\/s11734-024-01105-6","article-title":"Interaction of antimicrobial peptides with model membranes: A perspective towards new antibiotics","volume":"233","author":"Karmakar","year":"2024","journal-title":"Eur. Phys. J. Spec. Top."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"19446","DOI":"10.1073\/pnas.2005540117","article-title":"Two distinct amphipathic peptide antibiotics with systemic efficacy","volume":"117","author":"Narayana","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2424","DOI":"10.1016\/j.bpj.2015.04.006","article-title":"The structure of a melittin-stabilized pore","volume":"108","author":"Leveritt","year":"2015","journal-title":"Biophys. J."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2609","DOI":"10.1016\/j.apsb.2021.07.014","article-title":"Membrane-disruptive peptides\/peptidomimetics-based therapeutics: Promising systems to combat bacteria and cancer in the drug-resistant era","volume":"11","author":"Lin","year":"2021","journal-title":"Acta Pharm. Sin. B"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"10803","DOI":"10.3390\/molecules190810803","article-title":"Effects of single amino acid substitution on the biophysical properties and biological activities of an amphipathic alpha-helical antibacterial peptide against Gram-negative bacteria","volume":"19","author":"Tan","year":"2014","journal-title":"Molecules"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1016\/j.febslet.2013.03.039","article-title":"Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding","volume":"587","author":"Weber","year":"2013","journal-title":"FEBS Lett."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1128\/AAC.00925-06","article-title":"Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides","volume":"51","author":"Chen","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1264","DOI":"10.1002\/pro.5560060614","article-title":"The role of context on alpha-helix stabilization: Host-guest analysis in a mixed background peptide model","volume":"6","author":"Yang","year":"1997","journal-title":"Protein Sci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"8898","DOI":"10.1073\/pnas.84.24.8898","article-title":"Helix stabilization by Glu-\u2026Lys+ salt bridges in short peptides of de novo design","volume":"84","author":"Marqusee","year":"1987","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Roesgaard, M.A., Lundsgaard, J.E., Newcombe, E.A., Jacobsen, N.L., Pesce, F., Tranchant, E.E., Lindemose, S., Prestel, A., Hartmann-Petersen, R., and Lindorff-Larsen, K. (2022). Deciphering the Alphabet of Disorder-Glu and Asp Act Differently on Local but Not Global Properties. Biomolecules, 12.","DOI":"10.1101\/2022.08.25.505250"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1351\/pac200880061337","article-title":"On the solvent role in alcohol-induced \u03b1-helix formation of chymotrypsin inhibitor 2","volume":"80","author":"Yoshida","year":"2008","journal-title":"Pure Appl. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"12179","DOI":"10.1073\/pnas.182199699","article-title":"Mechanism by which 2,2,2-trifluoroethanol\/water mixtures stabilize secondary-structure formation in peptides: A molecular dynamics study","volume":"99","author":"Roccatano","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1016\/j.bbamem.2016.02.010","article-title":"Effect of dimerization on the mechanism of action of aurein 1.2","volume":"1858","author":"Lorenzon","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"D\u2019Accolti, M., Bellotti, D., Dzien, E., Leonetti, C., Leveraro, S., Albanese, V., Marzola, E., Guerrini, R., Caselli, E., and Rowinska-Zyrek, M. (2023). Impact of C- and N-terminal protection on the stability, metal chelation and antimicrobial properties of calcitermin. Sci. Rep., 13.","DOI":"10.1038\/s41598-023-45437-0"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1007\/s00249-015-1094-x","article-title":"The effect of amidation on the behaviour of antimicrobial peptides","volume":"45","author":"Mura","year":"2016","journal-title":"Eur. Biophys. J. Biophy."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Reinke, P.Y.A., Heiringhoff, R.S., Reindl, T., Baker, K., Taft, M.H., Meents, A., Mulvihill, D.P., Davies, O.R., Fedorov, R., and Zahn, M. (2024). Crystal structures of cables formed by the acetylated and unacetylated forms of the Schizosaccharomyces pombe tropomyosin ortholog TpmCdc8. J. Biol. Chem., 300.","DOI":"10.1016\/j.jbc.2024.107925"},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Al Musaimi, O., Lombardi, L., Williams, D.R., and Albericio, F. (2022). Strategies for Improving Peptide Stability and Delivery. Pharmaceuticals, 15.","DOI":"10.3390\/ph15101283"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2101","DOI":"10.1093\/bioinformatics\/btn392","article-title":"HELIQUEST: A web server to screen sequences with specific alpha-helical properties","volume":"24","author":"Gautier","year":"2008","journal-title":"Bioinformatics"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Takechi-Haraya, Y., Ohgita, T., Kotani, M., Kono, H., Saito, C., Tamagaki-Asahina, H., Nishitsuji, K., Uchimura, K., Sato, T., and Kawano, R. (2022). Effect of hydrophobic moment on membrane interaction and cell penetration of apolipoprotein E-derived arginine-rich amphipathic alpha-helical peptides. Sci. Rep., 12.","DOI":"10.1038\/s41598-022-08876-9"},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Luo, Y., and Song, Y. (2021). Mechanism of Antimicrobial Peptides: Antimicrobial, Anti-Inflammatory and Antibiofilm Activities. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222111401"},{"key":"ref_57","first-page":"1","article-title":"Envelope Structures of Gram-Positive Bacteria","volume":"Volume 404","author":"Bagnoli","year":"2017","journal-title":"Current Topics in Microbiology and Immunology"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Barreto-Santamar\u00eda, A., Ar\u00e9valo-Pinz\u00f3n, G., Patarroyo, M.A.A., and Patarroyo, M.E.E. (2021). How to Combat Gram-Negative Bacteria Using Antimicrobial Peptides: A Challenge or an Unattainable Goal?. Antibiotics, 10.","DOI":"10.3390\/antibiotics10121499"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"7570","DOI":"10.1021\/acs.jmedchem.3c00460","article-title":"To Fold or Not to Fold: Diastereomeric Optimization of an \u03b1-Helical Antimicrobial Peptide","volume":"66","author":"Personne","year":"2023","journal-title":"J. Med. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Liscano, Y., Salamanca, C.H., Vargas, L., Cantor, S., Laverde-Rojas, V., and O\u00f1ate-Garz\u00f3n, J. (2019). Increases in Hydrophilicity and Charge on the Polar Face of Alyteserin 1c Helix Change its Selectivity towards Gram-Positive Bacteria. 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