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Structural modifications of the natural antimicrobial peptides (AMPs) provide a straightforward approach to develop potent antimicrobial agents with high specificity and low toxicity. In this study, we truncated 11-amino-acids at the C-terminus of Pleurocidin, an AMP produced by Pleuronectes americanus, and obtained four peptide analogues termed GK-1, GK-2, GK-3 and GK-4. Minimum inhibitory concentration (MIC) tests showed that GK-1 obtained by direct truncation of Pleurocidin has no antibacterial activity, while GK-2, GK-3 and GK-4 show considerable antibacterial activity with Pleurocidin. Notably, GK-4 displays rapid bacteriostatic activity, great stability and low hemolysis, as well as enhanced hydrolytic resistance to pepsin treatment. Mechanistic studies showed that GK-4 induces membrane damage by interacting with bacterial membrane-specific components, dissipates bacterial membrane potential and promotes the generation of ROS. SEM and CD analysis further confirmed the ability of GK-4 to resist pepsin hydrolysis, which may be attributed to its stable helicity structure. Collectively, our findings reveal that GK-4 is a potential orally available candidate to treat infections caused by multidrug-resistant pathogens.<\/jats:p>","DOI":"10.3390\/pharmaceutics14102025","type":"journal-article","created":{"date-parts":[[2022,9,26]],"date-time":"2022-09-26T03:34:17Z","timestamp":1664163257000},"page":"2025","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Truncated Pleurocidin Derivative with High Pepsin Hydrolysis Resistance to Combat Multidrug-Resistant Pathogens"],"prefix":"10.3390","volume":"14","author":[{"given":"Dejuan","family":"Wang","sequence":"first","affiliation":[{"name":"College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jingru","family":"Shi","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chen","family":"Chen","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6486-9600","authenticated-orcid":false,"given":"Zhiqiang","family":"Wang","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China"},{"name":"Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou University, Yangzhou 225009, China"},{"name":"Joint International Research Laboratory of Agriculture and Agri-Product Safety, the Ministry of Education of China, Yangzhou University, Yangzhou 225009, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9622-6471","authenticated-orcid":false,"given":"Yuan","family":"Liu","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China"},{"name":"Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou University, Yangzhou 225009, China"},{"name":"Joint International Research Laboratory of Agriculture and Agri-Product Safety, the Ministry of Education of China, Yangzhou University, Yangzhou 225009, China"},{"name":"Institute of Comparative Medicine, Yangzhou University, Yangzhou 225009, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,9,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1038\/nrmicro3439","article-title":"Tackling antibiotic resistance: The environmental framework","volume":"13","author":"Berendonk","year":"2015","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_2","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":"ref_3","doi-asserted-by":"crossref","first-page":"113818","DOI":"10.1016\/j.addr.2021.05.028","article-title":"Antimicrobial peptides towards clinical application: Delivery and formulation","volume":"175","author":"Wang","year":"2021","journal-title":"Adv. Drug. Deliv. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"5085","DOI":"10.1021\/acs.jmedchem.2c00061","article-title":"Site-specific isopeptide bond formation: A powerful tool for the generation of potent and nontoxic antimicrobial peptides","volume":"65","author":"Wani","year":"2022","journal-title":"J. Med. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1038\/s41551-020-0556-3","article-title":"De novo development of proteolytically resistant therapeutic peptides for oral administration","volume":"4","author":"Kong","year":"2020","journal-title":"Nat. Biomed. Eng."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"eabk1792","DOI":"10.1126\/sciadv.abk1792","article-title":"Dynamic omnidirectional adhesive microneedle system for oral macromolecular drug delivery","volume":"8","author":"Chen","year":"2022","journal-title":"Sci. Adv."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"8094","DOI":"10.1021\/acs.chemrev.6b00838","article-title":"Orally absorbed cyclic peptides","volume":"117","author":"Nielsen","year":"2017","journal-title":"Chem. Rev."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.ejmech.2016.09.071","article-title":"Pyrazole derived ultra-short antimicrobial peptidomimetics with potent anti-biofilm activity","volume":"125","author":"Ahn","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.7150\/thno.39157","article-title":"Potent antibacterial activity of MSI-1 derived from the magainin 2 peptide against drug-resistant bacteria","volume":"10","author":"Ma","year":"2020","journal-title":"Theranostics"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1021\/acsinfecdis.8b00230","article-title":"Discovery of linear low-cationic peptides to target methicillin-resistant Staphylococcus aureus in vivo","volume":"5","author":"Liu","year":"2019","journal-title":"ACS Infect. Dis."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"McMillan, K.A.M., and Coombs, M.R.P. (2021). Investigating potential applications of the fish anti-microbial peptide pleurocidin: A systematic review. Pharmaceuticals, 14.","DOI":"10.3390\/ph14070687"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"7163","DOI":"10.1021\/acs.jpcb.1c01954","article-title":"Molecular insights into pore formation mechanism, membrane perturbation, and water permeation by the antimicrobial peptide pleurocidin: A combined all-atom and coarse-grained molecular dynamics simulation study","volume":"125","author":"Talandashti","year":"2021","journal-title":"J. Phys. Chem. B"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1038\/s42003-020-01420-3","article-title":"A pleurocidin analogue with greater conformational flexibility, enhanced antimicrobial potency and in vivo therapeutic efficacy","volume":"3","author":"Manzo","year":"2020","journal-title":"Commun. Biol."},{"key":"ref_14","unstructured":"Clinical and Laboratory Standards Institute (2018). Performance Standards for Antimicrobial Susceptibility Testing, CLSI."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Shi, J., Chen, C., Wang, D., Tong, Z., Wang, Z., and Liu, Y. (2021). Amphipathic peptide antibiotics with potent activity against multidrug-resistant pathogens. Pharmaceutics, 13.","DOI":"10.3390\/pharmaceutics13040438"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"26516","DOI":"10.1073\/pnas.1909585117","article-title":"The antimicrobial peptide ZY4 combats multidrug-resistant Pseudomonas aeruginosa and Acinetobacter baumannii infection","volume":"116","author":"Mwangi","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_17","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":"ref_18","doi-asserted-by":"crossref","unstructured":"Gonzalez Garcia, M., Rodriguez, A., Alba, A., Vazquez, A.A., Morales Vicente, F.E., Perez-Erviti, J., Spellerberg, B., Stenger, S., Grieshober, M., and Conzelmann, C. (2020). New antibacterial peptides from the freshwater mollusk Pomacea poeyana (Pilsbry, 1927). Biomolecules, 10.","DOI":"10.3390\/biom10111473"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/j.ejmech.2018.03.025","article-title":"Antimicrobial activity and self-assembly behavior of antimicrobial peptide chensinin-1b with lipophilic alkyl tails","volume":"150","author":"Dong","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"ref_20","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":"ref_21","doi-asserted-by":"crossref","unstructured":"Jayathilaka, E., Rajapaksha, D.C., Nikapitiya, C., De Zoysa, M., and Whang, I. (2021). Antimicrobial and anti-biofilm peptide octominin for controlling multidrug-resistant Acinetobacter baumannii. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22105353"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Hong, M.J., Kim, M.K., and Park, Y. (2021). Comparative antimicrobial activity of Hp404 peptide and its analogs against Acinetobacter baumannii. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22115540"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1667","DOI":"10.1038\/s41564-017-0037-y","article-title":"Contribution of reactive oxygen species to thymineless death in Escherichia coli","volume":"2","author":"Hong","year":"2017","journal-title":"Nat. Microbiol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"e2104211","DOI":"10.1002\/smll.202104211","article-title":"Human antimicrobial peptide triggered colloidal transformations in bacteria membrane lipopolysaccharides","volume":"18","author":"Hong","year":"2022","journal-title":"Small"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1093\/femsre\/fuv008","article-title":"Bacterial membrane lipids: Diversity in structures and pathways","volume":"40","author":"Sohlenkamp","year":"2016","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Hazam, P.K., Cheng, C.C., Hsieh, C.Y., Lin, W.C., Hsu, P.H., Chen, T.L., Lee, Y.T., and Chen, J.Y. (2022). Development of bactericidal peptides against multidrug-resistant Acinetobacter baumannii with enhanced stability and low toxicity. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23042191"},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Qi, S., Gao, B., and Zhu, S. (2022). A fungal defensin inhibiting bacterial cell-wall biosynthesis with non-hemolysis and serum stability. J. Fungi., 8.","DOI":"10.3390\/jof8020174"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"16854","DOI":"10.1021\/acs.jmedchem.1c01712","article-title":"Multifunctional antibiotic-host defense peptide conjugate kills bacteria, eradicates biofilms, and modulates the innate immune response","volume":"64","author":"Etayash","year":"2021","journal-title":"J. Med. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"e0131821","DOI":"10.1128\/Spectrum.01318-21","article-title":"In vitro and in vivo studies on the antibacterial activity and safety of a new antimicrobial peptide dermaseptin-AC","volume":"9","author":"Chen","year":"2021","journal-title":"Microbiol. Spectr."},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Safronova, V.N., Panteleev, P.V., Sukhanov, S.V., Toropygin, I.Y., Bolosov, I.A., and Ovchinnikova, T.V. (2022). Mechanism of action and therapeutic potential of the beta-hairpin antimicrobial peptide capitellacin from the marine polychaeta capitella teleta. Mar. Drugs, 20.","DOI":"10.3390\/md20030167"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"740620","DOI":"10.3389\/fimmu.2021.740620","article-title":"SSTP1, a host defense peptide, exploits the immunomodulatory il6 pathway to induce apoptosis in cancer cells","volume":"12","author":"Gopalakrishnan","year":"2021","journal-title":"Front. Immunol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"16062","DOI":"10.1021\/acsami.1c01643","article-title":"Structural disruptions of the outer membranes of gram-negative bacteria by rationally designed amphiphilic antimicrobial peptides","volume":"13","author":"Gong","year":"2021","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Gan, B.H., Cai, X., Javor, S., Kohler, T., and Reymond, J.L. (2020). Synergistic effect of propidium iodide and small molecule antibiotics with the antimicrobial peptide dendrimer g3kl against Gram-negative bacteria. Molecules, 25.","DOI":"10.3390\/molecules25235643"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1016\/j.chembiol.2013.07.006","article-title":"Collapsing the proton motive force to identify synergistic combinations against Staphylococcus aureus","volume":"20","author":"Farha","year":"2013","journal-title":"Chem. Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"708712","DOI":"10.3389\/fmicb.2021.708712","article-title":"Deciphering the antibacterial role of peptide from Bacillus subtilis subsp. spizizenii Ba49 against Staphylococcus aureus","volume":"12","author":"Taggar","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.mib.2014.06.008","article-title":"Reactive oxygen species and the bacterial response to lethal stress","volume":"21","author":"Zhao","year":"2014","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"108699","DOI":"10.1016\/j.intimp.2022.108699","article-title":"Tricalcium phosphate particles promote pyroptotic death of calvaria osteocytes through the ROS\/NLRP3\/Caspase-1 signaling axis in amouse osteolysis model","volume":"107","author":"Zhang","year":"2022","journal-title":"Int. Immunopharmacol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"52665","DOI":"10.1007\/s11356-021-17041-0","article-title":"4-[1-Ethyl-1-methylhexy]-phenol induces apoptosis and interrupts Ca(2+) homeostasis via ROS pathway in Sertoli TM4 cells","volume":"29","author":"Liu","year":"2022","journal-title":"Environ. Sci. Pollut. Res. Int."},{"key":"ref_39","first-page":"1","article-title":"Unnatural amino acids: Promising implications for the development of new antimicrobial peptides","volume":"7","author":"Wang","year":"2022","journal-title":"Crit. Rev. Microbiol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1365","DOI":"10.1038\/s41467-017-01447-x","article-title":"Self-assembling dipeptide antibacterial nanostructures with membrane disrupting activity","volume":"8","author":"Schnaider","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/j.biomaterials.2015.02.111","article-title":"Anti-endotoxic and antibacterial effects of a dermal substitute coated with host defense peptides","volume":"53","author":"Kasetty","year":"2015","journal-title":"Biomaterials"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"107901","DOI":"10.1016\/j.biotechadv.2021.107901","article-title":"Antimicrobial peptides: Promising alternatives over conventional capture ligands for biosensor-based detection of pathogenic bacteria","volume":"55","author":"Islam","year":"2022","journal-title":"Biotechnol. Adv."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1016\/j.biochi.2010.02.023","article-title":"Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity","volume":"92","author":"Takahashi","year":"2010","journal-title":"Biochimie"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.biomaterials.2014.11.052","article-title":"Synthetic beta-sheet forming peptide amphiphiles for treatment of fungal keratitis","volume":"43","author":"Wu","year":"2015","journal-title":"Biomaterials"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1038\/s41579-019-0294-2","article-title":"Porins and small-molecule translocation across the outer membrane of Gram-negative bacteria","volume":"18","author":"Vergalli","year":"2020","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.actbio.2015.11.002","article-title":"Short, multiple-stranded beta-hairpin peptides have antimicrobial potency with high selectivity and salt resistance","volume":"30","author":"Chou","year":"2016","journal-title":"Acta Biomater."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.tibtech.2011.05.001","article-title":"The expanding scope of antimicrobial peptide structures and their modes of action","volume":"29","author":"Nguyen","year":"2011","journal-title":"Trends Biotechnol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"6773","DOI":"10.1039\/D1SM00703C","article-title":"Investigating lipid headgroup composition within epithelial membranes: A systematic review","volume":"17","author":"Coones","year":"2021","journal-title":"Soft Matter"},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Liu, Y., Shi, J., Tong, Z., Jia, Y., Yang, K., and Wang, Z. (2020). Potent broad-spectrum antibacterial activity of amphiphilic peptides against multidrug-resistant bacteria. Microorganisms, 8.","DOI":"10.3390\/microorganisms8091398"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"746006","DOI":"10.3389\/fmicb.2021.746006","article-title":"A novel antimicrobial peptide Sparamosin26-54 from the mud crab scylla paramamosain showing potent antifungal activity against Cryptococcus neoformans","volume":"12","author":"Chen","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Xia, Y., Cebrian, R., Xu, C., Jong, A., Wu, W., and Kuipers, O.P. (2021). Elucidating the mechanism by which synthetic helper peptides sensitize Pseudomonas aeruginosa to multiple antibiotics. PLoS Pathog., 17.","DOI":"10.1371\/journal.ppat.1009909"}],"container-title":["Pharmaceutics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4923\/14\/10\/2025\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T00:37:59Z","timestamp":1760143079000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4923\/14\/10\/2025"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,9,23]]},"references-count":51,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2022,10]]}},"alternative-id":["pharmaceutics14102025"],"URL":"https:\/\/doi.org\/10.3390\/pharmaceutics14102025","relation":{},"ISSN":["1999-4923"],"issn-type":[{"value":"1999-4923","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,9,23]]}}}