{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T23:50:13Z","timestamp":1791330613927,"version":"4.3.1"},"reference-count":83,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["U21A20252"],"award-info":[{"award-number":["U21A20252"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32030101"],"award-info":[{"award-number":["32030101"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["U25A20708"],"award-info":[{"award-number":["U25A20708"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32002215"],"award-info":[{"award-number":["32002215"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100010009","name":"Heilongjiang Provincial Postdoctoral Science Foundation","doi-asserted-by":"publisher","award":["LBH-TZ2305"],"award-info":[{"award-number":["LBH-TZ2305"]}],"id":[{"id":"10.13039\/501100010009","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012548","name":"Heilongjiang Postdoctoral Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012548","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002858","name":"China Postdoctoral Science Foundation","doi-asserted-by":"publisher","award":["2021M690576"],"award-info":[{"award-number":["2021M690576"]}],"id":[{"id":"10.13039\/501100002858","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell Chemical Biology"],"published-print":{"date-parts":[[2026,9]]},"DOI":"10.1016\/j.chembiol.2026.09.001","type":"journal-article","created":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T15:22:52Z","timestamp":1790781772000},"update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Rational design of protease-resistant lipopeptides for combating antibiotic-resistant bacteria"],"prefix":"10.1016","author":[{"given":"Jiajun","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haoran","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Na","family":"Dong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weikang","family":"Yu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shiqi","family":"He","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anshan","family":"Shan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.chembiol.2026.09.001_bib1","doi-asserted-by":"crossref","first-page":"6997","DOI":"10.1039\/C8SC02616E","article-title":"Probing key elements of teixobactin-lipid II interactions in membranes","volume":"9","author":"Wen","year":"2018","journal-title":"Chem. Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib2","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pmed.1002184","article-title":"Will 10 Million People Die a Year due to Antimicrobial Resistance by 2050?","volume":"13","author":"de Kraker","year":"2016","journal-title":"PLoS Med."},{"key":"10.1016\/j.chembiol.2026.09.001_bib3","doi-asserted-by":"crossref","first-page":"5924","DOI":"10.2174\/0929867325666180713125314","article-title":"Antimicrobial Peptides: Amphibian Host Defense Peptides","volume":"26","author":"Patocka","year":"2019","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib4","doi-asserted-by":"crossref","first-page":"68","DOI":"10.3390\/ph11030068","article-title":"Bioinspired Designs, Molecular Premise and Tools for Evaluating the Ecological Importance of Antimicrobial Peptides","volume":"11","author":"Ongey","year":"2018","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.chembiol.2026.09.001_bib5","doi-asserted-by":"crossref","first-page":"2129","DOI":"10.1021\/acsami.9b19927","article-title":"Design of Heptad Repeat Amphiphiles Based on Database Filtering and Structure-Function Relationships to Combat Drug-Resistant Fungi and Biofilms","volume":"12","author":"Tan","year":"2020","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"10.1016\/j.chembiol.2026.09.001_bib6","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1002\/adhm.201800354","article-title":"From Antimicrobial Peptides to Antimicrobial Poly(alpha-amino acid)s","volume":"7","author":"Shen","year":"2018","journal-title":"Adv. Healthc. Mater."},{"key":"10.1016\/j.chembiol.2026.09.001_bib7","doi-asserted-by":"crossref","first-page":"6040","DOI":"10.1021\/acs.chemrev.8b00520","article-title":"Mechanistic Landscape of Membrane-Permeabilizing Peptides","volume":"119","author":"Guha","year":"2019","journal-title":"Chem. Rev."},{"key":"10.1016\/j.chembiol.2026.09.001_bib8","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1021\/acsinfecdis.9b00410","article-title":"Host Defense Peptide Mimicking Peptide Polymer Exerting Fast, Broad Spectrum, and Potent Activities toward Clinically Isolated Multidrug-Resistant Bacteria","volume":"6","author":"Chen","year":"2020","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.chembiol.2026.09.001_bib9","doi-asserted-by":"crossref","first-page":"2144","DOI":"10.1039\/C9BM00248K","article-title":"Host defense peptide mimicking poly-\u03b2-peptides with fast, potent and broad spectrum antibacterial activities","volume":"7","author":"Zhang","year":"2019","journal-title":"Biomater. Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib10","doi-asserted-by":"crossref","first-page":"381","DOI":"10.34133\/research.0381","article-title":"Cathelicidin-HG Alleviates Sepsis-Induced Platelet Dysfunction by Inhibiting GPVI-Mediated Platelet Activation","volume":"7","author":"Xiong","year":"2024","journal-title":"Research"},{"key":"10.1016\/j.chembiol.2026.09.001_bib11","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.00292-17","article-title":"Susceptibility of Colistin-Resistant, Gram-Negative Bacteria to Antimicrobial Peptides and Ceragenins","volume":"61","author":"Hashemi","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.chembiol.2026.09.001_bib12","doi-asserted-by":"crossref","first-page":"4673","DOI":"10.1128\/AAC.48.12.4673-4679.2004","article-title":"Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureus-derived proteinases","volume":"48","author":"Sieprawska-Lupa","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.chembiol.2026.09.001_bib13","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0045-2068(03)00080-4","article-title":"Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance","volume":"31","author":"Shinnar","year":"2003","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib14","doi-asserted-by":"crossref","DOI":"10.3390\/molecules25133048","article-title":"Towards Robust Delivery of Antimicrobial Peptides to Combat Bacterial Resistance","volume":"25","author":"Drayton","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/j.chembiol.2026.09.001_bib15","doi-asserted-by":"crossref","DOI":"10.3390\/biom8010004","article-title":"Antimicrobial Peptides: Diversity, Mechanism of Action and Strategies to Improve the Activity and Biocompatibility In Vivo","volume":"8","author":"Kumar","year":"2018","journal-title":"Biomolecules"},{"key":"10.1016\/j.chembiol.2026.09.001_bib16","doi-asserted-by":"crossref","first-page":"2286","DOI":"10.1021\/acs.jmedchem.8b01348","article-title":"Antimicrobial Peptides with High Proteolytic Resistance for Combating Gram-Negative Bacteria","volume":"62","author":"Wang","year":"2019","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib17","doi-asserted-by":"crossref","first-page":"8028","DOI":"10.1016\/j.biomaterials.2014.06.005","article-title":"Antimicrobial potency and selectivity of simplified symmetric-end peptides","volume":"35","author":"Dong","year":"2014","journal-title":"Biomaterials"},{"key":"10.1016\/j.chembiol.2026.09.001_bib18","series-title":"Specificity of Proteolysis","author":"Keil","year":"1992"},{"key":"10.1016\/j.chembiol.2026.09.001_bib19","doi-asserted-by":"crossref","first-page":"5558","DOI":"10.1021\/jm1006337","article-title":"Unnatural Amino Acid Side Chains as S1, S1 ', and S2 ' Probes Yield Cationic Antimicrobial Peptides with Stability toward Chymotryptic Degradation","volume":"53","author":"Karstad","year":"2010","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib20","doi-asserted-by":"crossref","first-page":"4501","DOI":"10.1021\/cr000033x","article-title":"Serine protease mechanism and specificity","volume":"102","author":"Hedstrom","year":"2002","journal-title":"Chem. Rev."},{"key":"10.1016\/j.chembiol.2026.09.001_bib21","doi-asserted-by":"crossref","first-page":"29987","DOI":"10.1074\/jbc.272.48.29987","article-title":"Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold","volume":"272","author":"Perona","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib22","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.bpc.2015.02.005","article-title":"N-terminal fatty acylation of peptides spanning the cationic C-terminal segment of bovine beta-defensin-2 results in salt-resistant antibacterial activity","volume":"199","author":"Krishnakumari","year":"2015","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib23","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1042\/BJ20041270","article-title":"Enhancement of endotoxin neutralization by coupling of a C12-alkyl chain to a lactoferricin-derived peptide","volume":"385","author":"Andr\u00e4","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.chembiol.2026.09.001_bib24","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/S0924-8579(02)00245-5","article-title":"The increased bactericidal activity of a fatty acid-modified synthetic antimicrobial peptide of human cathepsin G correlates with its enhanced capacity to interact with model membranes","volume":"21","author":"Mak","year":"2003","journal-title":"Int. J. Antimicrob. Agents"},{"key":"10.1016\/j.chembiol.2026.09.001_bib25","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1093\/jac\/dkg219","article-title":"Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain","volume":"51","author":"Majerle","year":"2003","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.chembiol.2026.09.001_bib26","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2019.111636","article-title":"Design and synthesis of new N-terminal fatty acid modified-antimicrobial peptide analogues with potent in vitro biological activity","volume":"182","author":"Zhong","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib27","doi-asserted-by":"crossref","DOI":"10.3390\/ijms21249692","article-title":"Lipidation of Antimicrobial Peptides as a Design Strategy for Future Alternatives to Antibiotics","volume":"21","author":"Rounds","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib28","doi-asserted-by":"crossref","first-page":"887","DOI":"10.3390\/ijms21030887","article-title":"Lipidated Analogs of the LL-37-Derived Peptide Fragment KR12 Structural Analysis, Surface-Active Properties and Antimicrobial Activity","volume":"21","author":"Kamysz","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib29","doi-asserted-by":"crossref","first-page":"6629","DOI":"10.1128\/AEM.01334-07","article-title":"Inhibition of fungal and bacterial plant pathogens in vitro and in planta with ultrashort cationic lipopeptides","volume":"73","author":"Makovitzki","year":"2007","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.chembiol.2026.09.001_bib30","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1016\/S0140-6736(97)80051-7","article-title":"Peptide antibiotics","volume":"349","author":"Hancock","year":"1997","journal-title":"Lancet"},{"key":"10.1016\/j.chembiol.2026.09.001_bib31","doi-asserted-by":"crossref","DOI":"10.1016\/j.drup.2023.101030","article-title":"Combating bacterial infections with host defense peptides: Shifting focus from bacteria to host immunity","volume":"72","author":"Gao","year":"2024","journal-title":"Drug Resist. Updat."},{"key":"10.1016\/j.chembiol.2026.09.001_bib32","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1038\/s41587-019-0222-z","article-title":"Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice","volume":"37","author":"Mourtada","year":"2019","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.chembiol.2026.09.001_bib33","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.jcis.2021.09.163","article-title":"Comparing pH-responsive nanogel swelling in dispersion and inside a polyacrylamide gel using photoluminescence spectroscopy and small-angle neutron scattering","volume":"608","author":"Zhu","year":"2022","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib34","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/j.actbio.2022.09.038","article-title":"Optimized proteolytic resistance motif (DabW)-based U1-2WD: A membrane-induced self-aggregating peptide to trigger bacterial agglutination and death","volume":"153","author":"He","year":"2022","journal-title":"Acta Biomater."},{"key":"10.1016\/j.chembiol.2026.09.001_bib35","doi-asserted-by":"crossref","first-page":"641","DOI":"10.2174\/0929866529666220613102145","article-title":"Antimicrobial Peptides: An Overview of their Structure, Function and Mechanism of Action","volume":"29","author":"Zhang","year":"2022","journal-title":"Protein Pept. Lett."},{"key":"10.1016\/j.chembiol.2026.09.001_bib36","doi-asserted-by":"crossref","first-page":"983","DOI":"10.3389\/fimmu.2020.00983","article-title":"Strategies in Translating the Therapeutic Potentials of Host Defense Peptides","volume":"11","author":"Ting","year":"2020","journal-title":"Front. Immunol."},{"key":"10.1016\/j.chembiol.2026.09.001_bib37","doi-asserted-by":"crossref","first-page":"2047","DOI":"10.4155\/fmc-2019-0167","article-title":"Antimicrobial peptides with protease stability: progress and perspective","volume":"11","author":"Shao","year":"2019","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib38","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1021\/bm401884e","article-title":"Effects of PEGylation on membrane and lipopolysaccharide interactions of host defense peptides","volume":"15","author":"Singh","year":"2014","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.chembiol.2026.09.001_bib39","doi-asserted-by":"crossref","first-page":"9140","DOI":"10.1021\/bi035948v","article-title":"Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan-containing hexapeptides","volume":"43","author":"Dathe","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2026.09.001_bib40","doi-asserted-by":"crossref","first-page":"2317","DOI":"10.1007\/s00018-011-0721-7","article-title":"Proline-rich antimicrobial peptides: converging to a non-lytic mechanism of action","volume":"68","author":"Scocchi","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib41","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1039\/C7NP00020K","article-title":"Proline-rich antimicrobial peptides targeting protein synthesis","volume":"34","author":"Graf","year":"2017","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.chembiol.2026.09.001_bib42","doi-asserted-by":"crossref","first-page":"7959","DOI":"10.3390\/ijms22157959","article-title":"Effects of Lipidation on a Proline-Rich Antibacterial Peptide","volume":"22","author":"Armas","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib43","doi-asserted-by":"crossref","first-page":"111","DOI":"10.3389\/fcell.2016.00111","article-title":"Antimicrobial Activity of Cationic Antimicrobial Peptides against Gram-Positives: Current Progress Made in Understanding the Mode of Action and the Response of Bacteria","volume":"4","author":"Omardien","year":"2016","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.chembiol.2026.09.001_bib44","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1111\/j.1747-0285.2010.00973.x","article-title":"Antimicrobial activity of short, synthetic cationic lipopeptides","volume":"75","author":"Laverty","year":"2010","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.chembiol.2026.09.001_bib45","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1021\/bc0341573","article-title":"Promotion of peptide antimicrobial activity by fatty acid conjugation","volume":"15","author":"Chu-Kung","year":"2004","journal-title":"Bioconjug. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib46","doi-asserted-by":"crossref","first-page":"4932","DOI":"10.1039\/D0CS01026J","article-title":"Chemically modified and conjugated antimicrobial peptides against superbugs","volume":"50","author":"Li","year":"2021","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.chembiol.2026.09.001_bib47","doi-asserted-by":"crossref","first-page":"2215","DOI":"10.1128\/AAC.01100-08","article-title":"Antibacterial activity of ultrashort cationic Lipo-\u03b2-peptides","volume":"53","author":"Serrano","year":"2009","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.chembiol.2026.09.001_bib48","doi-asserted-by":"crossref","first-page":"6412","DOI":"10.1021\/am401629p","article-title":"Immobilization Studies of an Engineered Arginine-Tryptophan Rich Peptide on a Silicone Surface with Antimicrobial and Antibiofilm Activity","volume":"5","author":"Lim","year":"2013","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"10.1016\/j.chembiol.2026.09.001_bib49","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.cocis.2010.05.006","article-title":"Interaction between amphiphilic peptides and phospholipid membranes","volume":"15","author":"Str\u00f6mstedt","year":"2010","journal-title":"Curr. Opin. Colloid Interface Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib50","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1016\/j.bbamem.2006.11.016","article-title":"Effects of topology, length, and charge on the activity of a kininogen-derived peptide on lipid membranes and bacteria","volume":"1768","author":"Ringstad","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.chembiol.2026.09.001_bib51","doi-asserted-by":"crossref","first-page":"5042","DOI":"10.1021\/la060317y","article-title":"Effect of peptide length on the interaction between consensus peptides and DOPC\/DOPA bilayers","volume":"22","author":"Ringstad","year":"2006","journal-title":"Langmuir"},{"key":"10.1016\/j.chembiol.2026.09.001_bib52","first-page":"1","article-title":"COLL 136-Composition effect on peptide interaction with lipids and bacteria: Variants of the C3a peptide CNY21. Abstr. Pap","volume":"232","author":"Ringstad","year":"2006","journal-title":"Am. Chem. Soc."},{"key":"10.1016\/j.chembiol.2026.09.001_bib53","doi-asserted-by":"crossref","first-page":"2898","DOI":"10.1128\/iai.65.7.2898-2903.1997","article-title":"Effects of pH and salinity on the antimicrobial properties of clavanins","volume":"65","author":"Lee","year":"1997","journal-title":"Infect. Immun."},{"key":"10.1016\/j.chembiol.2026.09.001_bib54","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1517\/13543784.16.8.1159","article-title":"Synthetic lipopeptides: a novel class of anti-infectives","volume":"16","author":"Jerala","year":"2007","journal-title":"Expert Opin. Investig. Drugs"},{"key":"10.1016\/j.chembiol.2026.09.001_bib55","doi-asserted-by":"crossref","first-page":"2254","DOI":"10.1021\/bi011549t","article-title":"Conjugation of a magainin analogue with lipophilic acids controls hydrophobicity, solution assembly, and cell selectivity","volume":"41","author":"Avrahami","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2026.09.001_bib56","first-page":"192","article-title":"A Comparative Study of the Antimicrobial and Structural Properties of Short Peptides and Lipopeptides Containing a Repetitive Motif KLFK. Protein Pept","volume":"26","author":"H\u00fampola","year":"2019","journal-title":"Lett"},{"key":"10.1016\/j.chembiol.2026.09.001_bib57","doi-asserted-by":"crossref","first-page":"1508","DOI":"10.1016\/j.bbamem.2009.04.002","article-title":"The role of fatty acid unsaturation in minimizing biophysical changes on the structure and local effects of bilayer membranes","volume":"1788","author":"Leekumjorn","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.chembiol.2026.09.001_bib58","doi-asserted-by":"crossref","first-page":"6533","DOI":"10.1021\/acs.jmedchem.5b00628","article-title":"N-Lipidated Peptide Dimers: Effective Antibacterial Agents against Gram-Negative Pathogens through Lipopolysaccharide Permeabilization","volume":"58","author":"Koh","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib59","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.ejmech.2014.06.003","article-title":"Tuning the antimicrobial pharmacophore to enable discovery of short lipopeptides with multiple modes of action","volume":"83","author":"Fang","year":"2014","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib60","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.cis.2013.06.009","article-title":"Effect of hydrophobic modifications in antimicrobial peptides","volume":"205","author":"Schmidtchen","year":"2014","journal-title":"Adv. Colloid Interface Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib61","first-page":"241","article-title":"Anti-tuberculosis activity of alpha-helical antimicrobial peptides: De novo designed L- and D-Enantiomers versus L- and D-LL37. Protein Pept","volume":"18","author":"Jiang","year":"2011","journal-title":"Lett"},{"key":"10.1016\/j.chembiol.2026.09.001_bib62","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1080\/22221751.2020.1754133","article-title":"Colistin and its role in the Era of antibiotic resistance: an extended review (2000-2019)","volume":"9","author":"El-Sayed Ahmed","year":"2020","journal-title":"Emerg. Microbes Infect."},{"key":"10.1016\/j.chembiol.2026.09.001_bib63","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1042\/BJ20050520","article-title":"Conjugation of fatty acids with different lengths modulates the antibacterial and antifungal activity of a cationic biologically inactive peptide","volume":"390","author":"Malina","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.chembiol.2026.09.001_bib64","doi-asserted-by":"crossref","first-page":"257","DOI":"10.3390\/molecules25020257","article-title":"Ultrashort Cationic Lipopeptides-Effect of N-Terminal Amino Acid and Fatty Acid Type on Antimicrobial Activity and Hemolysis","volume":"25","author":"Neubauer","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/j.chembiol.2026.09.001_bib65","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/j.jcis.2018.08.042","article-title":"Dependence on size and shape of non-nature amino acids in the enhancement of lipopolysaccharide (LPS) neutralizing activities of antimicrobial peptides","volume":"533","author":"Chih","year":"2019","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib66","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.plipres.2011.12.005","article-title":"Role of lipids in the interaction of antimicrobial peptides with membranes","volume":"51","author":"Teixeira","year":"2012","journal-title":"Prog. Lipid Res."},{"key":"10.1016\/j.chembiol.2026.09.001_bib67","doi-asserted-by":"crossref","first-page":"8173","DOI":"10.1073\/pnas.1509743112","article-title":"Antibiotic efficacy is linked to bacterial cellular respiration","volume":"112","author":"Lobritz","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.001_bib68","doi-asserted-by":"crossref","first-page":"2426","DOI":"10.1038\/s41396-023-01541-7","article-title":"Ginsenoside Rg3 enriches SCFA-producing commensal bacteria to confer protection against enteric viral infection via the cGAS-STING-type I IFN axis","volume":"17","author":"Wang","year":"2023","journal-title":"The ISME journal"},{"key":"10.1016\/j.chembiol.2026.09.001_bib69","doi-asserted-by":"crossref","first-page":"15106","DOI":"10.1021\/acs.langmuir.2c02118","article-title":"Growth of Prebiotically Plausible Fatty Acid Vesicles Proceeds in the Presence of Prebiotic Amino Acids, Dipeptides, Sugars, and Nucleic Acid Components","volume":"38","author":"Todd","year":"2022","journal-title":"Langmuir"},{"key":"10.1016\/j.chembiol.2026.09.001_bib70","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1038\/ni1001-907","article-title":"Nitric oxide and the immune response","volume":"2","author":"Bogdan","year":"2001","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.chembiol.2026.09.001_bib71","doi-asserted-by":"crossref","first-page":"5303","DOI":"10.1007\/s00018-021-03828-4","article-title":"Arginine-dependent immune responses","volume":"78","author":"Mart\u00ed I L\u00edndez","year":"2021","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib72","doi-asserted-by":"crossref","DOI":"10.3390\/ijms17111942","article-title":"Immunomodulatory Function of the Tumor Suppressor p53 in Host Immune Response and the Tumor Microenvironment","volume":"17","author":"Cui","year":"2016","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.chembiol.2026.09.001_bib73","doi-asserted-by":"crossref","DOI":"10.3390\/cancers10070219","article-title":"Role of p53 in the Regulation of the Inflammatory Tumor Microenvironment and Tumor Suppression","volume":"10","author":"Uehara","year":"2018","journal-title":"Cancers"},{"key":"10.1016\/j.chembiol.2026.09.001_bib74","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2020.569118","article-title":"Systematically Studying the Optimal Amino Acid Distribution Patterns of the Amphiphilic Structure by Using the Ultrashort Amphiphiles","volume":"11","author":"He","year":"2020","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.chembiol.2026.09.001_bib75","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/nature26157","article-title":"A new class of synthetic retinoid antibiotics effective against bacterial persisters","volume":"556","author":"Kim","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2026.09.001_bib76","doi-asserted-by":"crossref","first-page":"3782","DOI":"10.1021\/acs.jmedchem.9b00477","article-title":"Combating Drug-Resistant Fungi with Novel Imperfectly Amphipathic Palindromic Peptides","volume":"62","author":"Wang","year":"2019","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib77","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1093\/jac\/dkad022","article-title":"Pharmacokinetic and pharmacodynamic properties of polymyxin B in Escherichia coli and Klebsiella pneumoniae murine infection models","volume":"78","author":"van der Meijden","year":"2023","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.chembiol.2026.09.001_bib78","doi-asserted-by":"crossref","first-page":"4586","DOI":"10.1021\/acs.jmedchem.9b00149","article-title":"Rational Design of Short Peptide Variants by Using Kunitzin-RE, an Amphibian-Derived Bioactivity Peptide, for Acquired Potent Broad-Spectrum Antimicrobial and Improved Therapeutic Potential of Commensalism Coinfection of Pathogens","volume":"62","author":"Yang","year":"2019","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2026.09.001_bib79","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.biomaterials.2015.02.063","article-title":"Characterization of cell selectivity, physiological stability and endotoxin neutralization capabilities of alpha-helix-based peptide amphiphiles","volume":"52","author":"Ma","year":"2015","journal-title":"Biomaterials"},{"key":"10.1016\/j.chembiol.2026.09.001_bib80","doi-asserted-by":"crossref","first-page":"16529","DOI":"10.1073\/pnas.1904700116","article-title":"A selective membrane-targeting repurposed antibiotic with activity against persistent methicillin-resistant Staphylococcus aureus","volume":"116","author":"Kim","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.001_bib81","doi-asserted-by":"crossref","first-page":"2832","DOI":"10.3389\/fmicb.2018.02832","article-title":"Short Symmetric-End Antimicrobia Peptides Centered on beta-Turn Amino Acids Unit Improve Selectivity and Stability","volume":"9","author":"Dong","year":"2018","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.chembiol.2026.09.001_bib82","article-title":"Cross-Strand Interaction, Central Bending, and Sequence Pattern Act as Biomodulators of Simplified beta-Hairpin Antimicrobial Amphiphiles","volume":"17","author":"Shao","year":"2021","journal-title":"Small"},{"key":"10.1016\/j.chembiol.2026.09.001_bib83","doi-asserted-by":"crossref","first-page":"22113","DOI":"10.1021\/acsami.9b04654","article-title":"Highly Stabilized alpha-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition","volume":"11","author":"Lai","year":"2019","journal-title":"ACS Appl. Mater. Interfaces"}],"container-title":["Cell Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2451945626003296?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2451945626003296?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T22:57:10Z","timestamp":1791327430000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2451945626003296"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9]]},"references-count":83,"alternative-id":["S2451945626003296"],"URL":"https:\/\/doi.org\/10.1016\/j.chembiol.2026.09.001","relation":{},"ISSN":["2451-9456"],"issn-type":[{"value":"2451-9456","type":"print"}],"subject":[],"published":{"date-parts":[[2026,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Rational design of protease-resistant lipopeptides for combating antibiotic-resistant bacteria","name":"articletitle","label":"Article Title"},{"value":"Cell Chemical Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.chembiol.2026.09.001","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}