{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T17:27:14Z","timestamp":1782840434189,"version":"3.54.5"},"reference-count":69,"publisher":"Springer Science and Business Media LLC","issue":"10","license":[{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["World J Microbiol Biotechnol"],"published-print":{"date-parts":[[2025,10]]},"DOI":"10.1007\/s11274-025-04618-x","type":"journal-article","created":{"date-parts":[[2025,10,16]],"date-time":"2025-10-16T10:20:39Z","timestamp":1760610039000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Recombinant expression and functional characterization of defensin-like peptide TEWP and its analogs in Pichia pastoris"],"prefix":"10.1007","volume":"41","author":[{"given":"Saime G\u00fcls\u00fcm","family":"Batman","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Z\u00fclal","family":"Kesmen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,10,16]]},"reference":[{"key":"4618_CR1","doi-asserted-by":"publisher","DOI":"10.1111\/jfbc.12546","author":"TAE Ahmed","year":"2018","unstructured":"Ahmed TAE, Hammami R (2018) Recent insights into structure\u2013function relationships of antimicrobial peptides. J Food Biochem e12546. https:\/\/doi.org\/10.1111\/jfbc.12546","journal-title":"J Food Biochem e12546"},{"key":"4618_CR2","doi-asserted-by":"publisher","first-page":"233","DOI":"10.2165\/00063030-200317040-00002","volume":"17","author":"JP Bradshaw","year":"2003","unstructured":"Bradshaw JP (2003) Cationic antimicrobial peptides: issues for potential clinical use. BioDrugs 17:233\u2013240. https:\/\/doi.org\/10.2165\/00063030-200317040-00002","journal-title":"BioDrugs"},{"key":"4618_CR3","doi-asserted-by":"publisher","unstructured":"Bruggeman M, Ijakipour H, Stamboulis A (2019) Defensin-Like peptides and their antimicrobial activity in Free-Form and immobilized on material surfaces. Pept Synthesis Intechopen 66713. https:\/\/doi.org\/10.5772\/intechopen.85508","DOI":"10.5772\/intechopen.85508"},{"issue":"3","key":"4618_CR4","doi-asserted-by":"publisher","first-page":"1573","DOI":"10.1111\/jam.15315","volume":"132","author":"ME B\u00fcy\u00fckkiraz","year":"2021","unstructured":"B\u00fcy\u00fckkiraz ME, Kesmen Z (2021) Antimicrobial peptides (AMPs): A promising class of antimicrobial compounds. J Appl Microbiol 132(3):1573\u20131596. https:\/\/doi.org\/10.1111\/jam.15315","journal-title":"J Appl Microbiol"},{"key":"4618_CR5","doi-asserted-by":"publisher","first-page":"1998","DOI":"10.1002\/bab.2262","volume":"69","author":"ME B\u00fcy\u00fckkiraz","year":"2022","unstructured":"B\u00fcy\u00fckkiraz ME, Kesmen Z (2022) Recombinant expression and coexpression of oyster defensin and proline-rich peptide in Komagataella phaffii. Biotechnol Appl Biochem 69:1998\u20132007. https:\/\/doi.org\/10.1002\/bab.2262","journal-title":"Biotechnol Appl Biochem"},{"key":"4618_CR6","doi-asserted-by":"publisher","first-page":"1184","DOI":"10.1016\/j.bbamem.2006.04.006","volume":"1758","author":"DI Chan","year":"2006","unstructured":"Chan DI, Prenner EJ, Vogel HJ (2006) Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action. Biochim Biophys Acta 1758:1184\u20131202. https:\/\/doi.org\/10.1016\/j.bbamem.2006.04.006","journal-title":"Biochim Biophys Acta"},{"key":"4618_CR7","doi-asserted-by":"publisher","first-page":"524","DOI":"10.1002\/prot.20963","volume":"64","author":"S Chattopadhyay","year":"2006","unstructured":"Chattopadhyay S, Sinha NK, Banerjee S, Roy D, Chattopadhyay D, Roy S (2006) Small cationic protein from a marine turtle has \u03b2-defensin-like fold and antibacterial and antiviral activity. Proteins 64:524\u2013531. https:\/\/doi.org\/10.1002\/prot.20963","journal-title":"Proteins"},{"issue":"4","key":"4618_CR8","doi-asserted-by":"publisher","first-page":"1398","DOI":"10.1128\/aac.00925-06","volume":"51","author":"Y Chen","year":"2007","unstructured":"Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS (2007) Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides. Antimicrob Agents Chemother 51(4):1398\u20131406. https:\/\/doi.org\/10.1128\/aac.00925-06","journal-title":"Antimicrob Agents Chemother"},{"key":"4618_CR9","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1007\/s00253-010-2864-0","volume":"89","author":"Z Chen","year":"2011","unstructured":"Chen Z, Wang D, Cong Y, Wang J, Zhu J, Yang J, Hu Z, Hu X, Tan Y, Hu F, Rao X (2011) Recombinant antimicrobial peptide hPAB-\u03b2 expressed in Pichia pastoris, a potential agent active against methicillin-resistant Staphylococcus aureus. Appl Microbiol Biotechnol 89:281\u2013291. https:\/\/doi.org\/10.1007\/s00253-010-2864-0","journal-title":"Appl Microbiol Biotechnol"},{"issue":"4","key":"4618_CR10","doi-asserted-by":"publisher","first-page":"757","DOI":"10.1111\/1751-7915.14213","volume":"16","author":"MG Ciulla","year":"2023","unstructured":"Ciulla MG, Gelain F (2023) Structure-activity relationships of antibacterial peptides. Microb Biotechnol 16(4):757\u2013777. https:\/\/doi.org\/10.1111\/1751-7915.14213","journal-title":"Microb Biotechnol"},{"key":"4618_CR11","doi-asserted-by":"publisher","first-page":"605","DOI":"10.1038\/s42003-021-02137-7","volume":"4","author":"S Clark","year":"2021","unstructured":"Clark S, Jowitt TA, Harris LK, Knight CG, Dobson CB (2021) The lexicon of antimicrobial peptides: A complete set of arginine and Tryptophan sequences. Commun Biol 4:605. https:\/\/doi.org\/10.1038\/s42003-021-02137-7","journal-title":"Commun Biol"},{"key":"4618_CR12","doi-asserted-by":"publisher","first-page":"146","DOI":"10.1016\/S0014-5793(01)02648-5","volume":"501","author":"M Dathe","year":"2001","unstructured":"Dathe M, Nikolenko H, Meyer J, Beyermann M, Bienert M (2001) Optimization of the antimicrobial activity of Magainin peptides by modification of charge. FEBS Lett 501:146\u2013150. https:\/\/doi.org\/10.1016\/S0014-5793(01)02648-5","journal-title":"FEBS Lett"},{"key":"4618_CR13","doi-asserted-by":"publisher","first-page":"1543","DOI":"10.1016\/j.febslet.2010.03.004","volume":"584","author":"E De Leeuw","year":"2010","unstructured":"De Leeuw E, Li C, Zeng P, Li C, Buin MD-d, Lu W-Y, Breukink E, Lu W (2010) Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II. FEBS Lett 584:1543\u20131548. https:\/\/doi.org\/10.1016\/j.febslet.2010.03.004","journal-title":"FEBS Lett"},{"key":"4618_CR14","doi-asserted-by":"publisher","first-page":"164","DOI":"10.1186\/s12934-023-02164-5","volume":"22","author":"C Dong","year":"2023","unstructured":"Dong C, Xu L, Lu W, Li M, Zhang R, Sun Y, Liu J, Chu X (2023) Antibacterial peptide PMAP-37(F34-R), expressed in Pichia pastoris, is effective against pathogenic bacteria and preserves plums. Microb Cell Fact 22:164. https:\/\/doi.org\/10.1186\/s12934-023-02164-5","journal-title":"Microb Cell Fact"},{"key":"4618_CR15","doi-asserted-by":"publisher","first-page":"8677","DOI":"10.3390\/ijms22168677","volume":"22","author":"N Doti","year":"2021","unstructured":"Doti N, Mardirossian M, Sandomenico A, Ruvo M, Caporale A (2021) Recent applications of Retro-Inverso peptides. Int J Mol Sci 22:8677. https:\/\/doi.org\/10.3390\/ijms22168677","journal-title":"Int J Mol Sci"},{"key":"4618_CR16","doi-asserted-by":"publisher","first-page":"761","DOI":"10.1038\/s41594-019-0291-1","volume":"26","author":"M Eldeeb","year":"2019","unstructured":"Eldeeb M, Esmaili M, Fahlman R (2019) Degradation of proteins with N-terminal Glycine. Nat Struct Mol Biol 26:761\u2013763. https:\/\/doi.org\/10.1038\/s41594-019-0291-1","journal-title":"Nat Struct Mol Biol"},{"key":"4618_CR17","doi-asserted-by":"publisher","unstructured":"Falanga A, Nigro E, De Biasi MG, Daniele A, Morelli G, Galdiero S, Scudiero O (2017) Cyclic peptides as novel therapeutic microbicides: engineering of human defensin mimetics. Molecules 22(7). https:\/\/doi.org\/10.3390\/molecules22071217","DOI":"10.3390\/molecules22071217"},{"issue":"1","key":"4618_CR18","doi-asserted-by":"publisher","first-page":"801","DOI":"10.1007\/s10989-020-10127-2","volume":"27","author":"BS Fazly Bazzaz","year":"2021","unstructured":"Fazly Bazzaz BS, Seyedi S, Hoseini Goki N, Khameneh B (2021) Human antimicrobial peptides: spectrum, mode of action and resistance mechanisms. Int J Pept Res Ther 27(1):801\u2013816. https:\/\/doi.org\/10.1007\/s10989-020-10127-2","journal-title":"Int J Pept Res Ther"},{"issue":"1","key":"4618_CR19","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1038\/nrd3591","volume":"11","author":"CD Fjell","year":"2012","unstructured":"Fjell CD, Hiss JA, Hancock RE, Schneider G (2012) Designing antimicrobial peptides: form follows function. Nat Rev Drug Discovery 11(1):37\u201351. https:\/\/doi.org\/10.1038\/nrd3591","journal-title":"Nat Rev Drug Discovery"},{"issue":"1","key":"4618_CR20","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1038\/s41392-023-01553-x","volume":"8","author":"J Fu","year":"2023","unstructured":"Fu J, Zong X, Jin M, Min J, Wang F, Wang Y (2023) Mechanisms and regulation of defensins in host defense. Signal Transduct Target Therapy 8(1):300. https:\/\/doi.org\/10.1038\/s41392-023-01553-x","journal-title":"Signal Transduct Target Therapy"},{"issue":"19","key":"4618_CR21","doi-asserted-by":"publisher","first-page":"10821","DOI":"10.3390\/ijms251910821","volume":"25","author":"P Gagat","year":"2024","unstructured":"Gagat P, Ostr\u00f3wka M, Duda-Madej A, Mackiewicz P (2024) Enhancing antimicrobial peptide activity through modifications of charge, hydrophobicity, and structure. Int J Mol Sci 25(19):10821. https:\/\/doi.org\/10.3390\/ijms251910821","journal-title":"Int J Mol Sci"},{"issue":"9","key":"4618_CR22","doi-asserted-by":"publisher","first-page":"710","DOI":"10.1038\/nri1180","volume":"3","author":"T Ganz","year":"2003","unstructured":"Ganz T (2003) Defensins: antimicrobial peptides of innate immunity. Nat Rev Immunol 3(9):710\u2013720. https:\/\/doi.org\/10.1038\/nri1180","journal-title":"Nat Rev Immunol"},{"issue":"22","key":"4618_CR23","doi-asserted-by":"publisher","first-page":"3577","DOI":"10.1039\/B710425A","volume":"5","author":"J Garner","year":"2007","unstructured":"Garner J, Harding MM (2007) Design and synthesis of \u03b1-helical peptides and mimetics. Org Biomol Chem 5(22):3577\u20133585. https:\/\/doi.org\/10.1039\/B710425A","journal-title":"Org Biomol Chem"},{"key":"4618_CR24","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1002\/psc.1369","volume":"17","author":"R Gopal","year":"2011","unstructured":"Gopal R, Kim YJ, Seo CH, Hahm KS, Park Y (2011) Reversed sequence enhances antimicrobial activity of a synthetic peptide. J Pept Sci 17:329\u2013334. https:\/\/doi.org\/10.1002\/psc.1369","journal-title":"J Pept Sci"},{"key":"4618_CR25","doi-asserted-by":"publisher","first-page":"170666","DOI":"10.1016\/j.peptides.2021.170666","volume":"146","author":"Y Han","year":"2021","unstructured":"Han Y, Zhang M, Lai R, Zhang Z (2021) Chemical modifications to increase the therapeutic potential of antimicrobial peptides. Peptides 146:170666. https:\/\/doi.org\/10.1016\/j.peptides.2021.170666","journal-title":"Peptides"},{"key":"4618_CR26","doi-asserted-by":"publisher","first-page":"969","DOI":"10.1016\/j.chembiol.2017.07.010","volume":"24","author":"EF Haney","year":"2017","unstructured":"Haney EF, Wu BC, Lee K, Hilchie AL, Hancock R (2017) Aggregation and its influence on the Immunomodulatory activity of synthetic innate defense regulator peptides. Cell Chem Biol 24:969\u2013980 e4. https:\/\/doi.org\/10.1016\/j.chembiol.2017.07.010","journal-title":"Cell Chem Biol"},{"key":"4618_CR27","doi-asserted-by":"publisher","first-page":"115131","DOI":"10.1016\/j.ejmech.2023.115131","volume":"249","author":"PK Hazam","year":"2023","unstructured":"Hazam PK, Cheng CC, Lin WC, Hsieh CY, Hsu PH, Chen YR, \u2026 and, Chen JY (2023) Strategic modification of low-activity natural antimicrobial peptides confers antibacterial potential in vitro and in vivo. Eur J Med Chem 249:115131. https:\/\/doi.org\/10.1016\/j.ejmech.2023.115131","journal-title":"Eur J Med Chem"},{"issue":"12","key":"4618_CR28","doi-asserted-by":"publisher","first-page":"3147","DOI":"10.1021\/acsinfecdis.0c00264","volume":"6","author":"S Huo","year":"2020","unstructured":"Huo S, Chen C, Lyu Z, Zhang S, Wang Y, Nie B, Yue B (2020) Overcoming planktonic and intracellular Staphylococcus aureus-Associated infection with a Cell-Penetrating peptide-Conjugated antimicrobial peptide. ACS Infect Dis 6(12):3147\u20133162. https:\/\/doi.org\/10.1021\/acsinfecdis.0c00264","journal-title":"ACS Infect Dis"},{"issue":"2","key":"4618_CR29","doi-asserted-by":"publisher","first-page":"1096","DOI":"10.1007\/s12010-022-04210-1","volume":"195","author":"N Jangpromma","year":"2023","unstructured":"Jangpromma N, Konkchaiyaphum M, Punpad A, Sosiangdi S, Daduang S, Klaynongsruang S, Tankrathok A (2023) Rational design of RN15m4 Cathelin domain-based peptides from Siamese crocodile Cathelicidin improves antimicrobial activity. Appl Biochem Biotechnol 195(2):1096\u20131108. https:\/\/doi.org\/10.1007\/s12010-022-04210-1","journal-title":"Appl Biochem Biotechnol"},{"key":"4618_CR30","doi-asserted-by":"publisher","unstructured":"J\u00e4rv\u00e5 M, Lay FT, Phan TK, Humble C, Poon IK, Bleackley MR, Kvansakul M (2018) X-ray structure of a carpet-like antimicrobial defensin\u2013phospholipid membrane disruption complex. Nature communications, 9(1), 1962. https:\/\/doi.org\/10.1038\/s41467-018-04434-y","DOI":"10.1038\/s41467-018-04434-y"},{"issue":"3","key":"4618_CR31","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1002\/bip.20911","volume":"90","author":"Z Jiang","year":"2008","unstructured":"Jiang Z, Vasil AI, Hale JD, Hancock RE, Vasil ML, Hodges RS (2008) Effects of net charge and the number of positively charged residues on the biological activity of amphipathic \u03b1-helical cationic antimicrobial peptides. Pept Sci 90(3):369\u2013383. https:\/\/doi.org\/10.1002\/bip.20911","journal-title":"Pept Sci"},{"key":"4618_CR32","doi-asserted-by":"publisher","unstructured":"Jindal MH, Le CF, Mohd Yusof MY, Sekaran SD (2014) Net charge, hydrophobicity and specific amino acids contribute to the activity of antimicrobial peptides. Jummec 17(1). https:\/\/doi.org\/10.22452\/jummec.vol17no1.1","DOI":"10.22452\/jummec.vol17no1.1"},{"issue":"11","key":"4618_CR33","doi-asserted-by":"publisher","first-page":"1227","DOI":"10.1080\/17425247.2019.1676720","volume":"16","author":"K Kardani","year":"2019","unstructured":"Kardani K, Milani A, Shabani SH, Bolhassani A (2019) Cell penetrating peptides: the potent multi-cargo intracellular carriers. Expert Opin Drug Deliv 16(11):1227\u20131258. https:\/\/doi.org\/10.1080\/17425247.2019.1676720","journal-title":"Expert Opin Drug Deliv"},{"issue":"14","key":"4618_CR34","doi-asserted-by":"publisher","first-page":"4288","DOI":"10.1128\/AEM.00558-16","volume":"82","author":"J Kraszewska","year":"2016","unstructured":"Kraszewska J, Beckett MC, James TC, Bond U (2016) Comparative analysis of the antimicrobial activities of plant Defensin-Like and ultrashort peptides against Food- spoiling bacteria. Appl Environ Microbiol 82(14):4288\u20134298. https:\/\/doi.org\/10.1128\/AEM.00558-16","journal-title":"Appl Environ Microbiol"},{"key":"4618_CR35","doi-asserted-by":"publisher","first-page":"16723","DOI":"10.3390\/ijms242316723","volume":"24","author":"SV Kravchenko","year":"2023","unstructured":"Kravchenko SV, Domnin PA, Grishin SY, Vershinin NA, Gurina EV, Zakharova AA, Azev VN, Mustaeva LG, Gorbunova EY, Kobyakova MI (2023) Enhancing the antimicrobial properties of peptides through Cell-Penetrating peptide conjugation: A comprehensive assessment. Int J Mol Sci 24:16723. https:\/\/doi.org\/10.3390\/ijms242316723","journal-title":"Int J Mol Sci"},{"issue":"1","key":"4618_CR36","doi-asserted-by":"publisher","first-page":"4","DOI":"10.3390\/biom8010004","volume":"8","author":"P Kumar","year":"2018","unstructured":"Kumar P, Kizhakkedathu NJ, Straus SK (2018) Antimicrobial peptides: Diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo. Biomolecules 8(1):4. https:\/\/doi.org\/10.3390\/biom8010004","journal-title":"Biomolecules"},{"issue":"13","key":"4618_CR37","doi-asserted-by":"publisher","first-page":"15694","DOI":"10.1021\/acsomega.9b02278","volume":"4","author":"H Lee","year":"2019","unstructured":"Lee H, Lim SI, Shin SH, Lim Y, Koh JW, Yang S (2019) Conjugation of cell-penetrating peptides to antimicrobial peptides enhances antibacterial activity. ACS Omega 4(13):15694\u201315701. https:\/\/doi.org\/10.1021\/acsomega.9b02278","journal-title":"ACS Omega"},{"issue":"1","key":"4618_CR38","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1186\/s40529-021-00312-x","volume":"62","author":"J Li","year":"2021","unstructured":"Li J, Hu S, Jian W, Xie C, Yang X (2021) Plant antimicrobial peptides: structures, functions, and applications. Bot Stud 62(1):5. https:\/\/doi.org\/10.1186\/s40529-021-00312-x","journal-title":"Bot Stud"},{"issue":"1","key":"4618_CR39","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1016\/j.flm.2018.04.001","volume":"2","author":"Z Liu","year":"2018","unstructured":"Liu Z, Zhu M, Chen X, Yang G, Yang T, Yu L, Wang X (2018) Expression and antibacterial activity of hybrid antimicrobial peptide cecropinA-thanatin in Pichia pastoris. Front Lab Med 2(1):23\u201329. https:\/\/doi.org\/10.1016\/j.flm.2018.04.001","journal-title":"Front Lab Med"},{"key":"4618_CR40","doi-asserted-by":"publisher","first-page":"e01821","DOI":"10.1128\/mbio.01821-19","volume":"10","author":"K Loth","year":"2019","unstructured":"Loth K, Vergnes A, Barreto C, Voisin SN, Meudal H, Da Silva J et al (2019) The ancestral N-terminal domain of big defensins drives bacterially triggered assembly into antimicrobial nanonets. mBio 10:e01821\u2013e01819. https:\/\/doi.org\/10.1128\/mbio.01821-19","journal-title":"mBio"},{"key":"4618_CR41","doi-asserted-by":"publisher","first-page":"128","DOI":"10.1016\/j.peptides.2015.07.009","volume":"71","author":"B Mathew","year":"2015","unstructured":"Mathew B, Nagaraj R (2015) Antimicrobial activity of human \u03b1-defensin 5 and its linear analogs: N-terminal fatty acylation results in enhanced antimicrobial activity of the linear analogs. Peptides 71:128\u2013140. https:\/\/doi.org\/10.1016\/j.peptides.2015.07.009","journal-title":"Peptides"},{"key":"4618_CR42","doi-asserted-by":"publisher","first-page":"90","DOI":"10.1016\/j.pep.2016.10.003","volume":"130","author":"DM Meng","year":"2017","unstructured":"Meng DM, Zhao JF, Ling X, Dai HX, Guo YJ, Gao XF, Dong B, Zhang ZQ, Meng X, Fan ZC (2017) Recombinant expression, purification and antimicrobial activity of a novel antimicrobial peptide PaDef in Pichia pastoris. Protein Expr Purif 130:90\u201399. https:\/\/doi.org\/10.1016\/j.pep.2016.10.003","journal-title":"Protein Expr Purif"},{"key":"4618_CR43","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1016\/j.pep.2018.03.001","volume":"147","author":"DM Meng","year":"2018","unstructured":"Meng DM, Lv YJ, Zhao JF, Liu QY, Shi LY, Wang JP, Yang YH, Fan ZC (2018) Efficient production of a Recombinant Venerupis philippinarum defensin (VpDef) in Pichia pastoris and characterization of its antibacterial activity and stability. Protein Expr Purif 147:78\u201384. https:\/\/doi.org\/10.1016\/j.pep.2018.03.001","journal-title":"Protein Expr Purif"},{"key":"4618_CR44","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.pep.2019.03.007","volume":"160","author":"DM Meng","year":"2019","unstructured":"Meng DM, Li WJ, Shi LY, Lv YJ, Sun XQ, Hu JC, Fan ZC (2019) Expression, purification and characterization of a Recombinant antimicrobial peptide Hispidalin in Pichia pastoris. Protein Expr Purif 160:19\u201327. https:\/\/doi.org\/10.1016\/j.pep.2019.03.007","journal-title":"Protein Expr Purif"},{"key":"4618_CR45","doi-asserted-by":"publisher","first-page":"366","DOI":"10.3390\/ph8030366","volume":"8","author":"B Mojsoska","year":"2015","unstructured":"Mojsoska B, Jenssen H (2015) Peptides and peptidomimetics for antimicrobial drug design. Pharmaceuticals 8:366\u2013415. https:\/\/doi.org\/10.3390\/ph8030366","journal-title":"Pharmaceuticals"},{"key":"4618_CR46","doi-asserted-by":"publisher","first-page":"832","DOI":"10.1016\/j.peptides.2009.01.015","volume":"30","author":"HY Nan","year":"2009","unstructured":"Nan HY, Bang J, Shin SY (2009) Design of novel indolicidin-derived antimicrobial peptide with enhanced cell specificity and potent anti-inflammatory activity. Peptides 30:832\u2013838. https:\/\/doi.org\/10.1016\/j.peptides.2009.01.015","journal-title":"Peptides"},{"issue":"10","key":"4618_CR47","doi-asserted-by":"publisher","first-page":"1755","DOI":"10.1007\/s00726-017-2473-7","volume":"49","author":"D Neubauer","year":"2017","unstructured":"Neubauer D, Ja\u015bkiewicz M, Migo\u0144 D, Bauer M, Sikora K, Sikorska E, Kamysz E, Kamysz W (2017) Retro analog concept: comparative study on physico-chemical and biological properties of selected antimicrobial peptides. Amino Acids 49(10):1755\u20131771. https:\/\/doi.org\/10.1007\/s00726-017-2473-7","journal-title":"Amino Acids"},{"key":"4618_CR48","doi-asserted-by":"publisher","first-page":"464","DOI":"10.1016\/j.tibtech.2011.05.001","volume":"29","author":"LT Nguyen","year":"2011","unstructured":"Nguyen LT, Haney EF, Vogel HJ (2011) The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol 29:464\u2013472. https:\/\/doi.org\/10.1016\/j.tibtech.2011.05.001","journal-title":"Trends Biotechnol"},{"key":"4618_CR49","doi-asserted-by":"publisher","first-page":"1205","DOI":"10.1007\/s10989-021-10161-8","volume":"27","author":"S Nooranian","year":"2021","unstructured":"Nooranian S, Oskuee RK, Jalili A (2021) Antimicrobial peptides, a pool for novel cell penetrating peptides development and vice versa. Int J Pept Res Ther 27:1205\u20131220. https:\/\/doi.org\/10.1007\/s10989-021-10161-8","journal-title":"Int J Pept Res Ther"},{"key":"4618_CR50","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1016\/j.bbrc.2012.09.030","volume":"427","author":"HA Rydberg","year":"2012","unstructured":"Rydberg HA, Carlsson C, Nord\u00e9n B (2012) Membrane interaction and secondary structure of de Novo designed arginine- and Tryptophan peptides with dual function. Biochem Biophys Res Commun 427:261\u2013265. https:\/\/doi.org\/10.1016\/j.bbrc.2012.09.030","journal-title":"Biochem Biophys Res Commun"},{"key":"4618_CR51","doi-asserted-by":"publisher","first-page":"293","DOI":"10.1016\/j.jconrel.2012.09.019","volume":"163","author":"F Salomone","year":"2012","unstructured":"Salomone F, Cardarelli F, Luca MD, Boccardi C, Nifos\u00ec R, Bardi G, Bari LD, Serresi M, Beltram F (2012) A novel chimeric cell-penetrating peptide with membrane-disruptive properties for efficient endosomal escape. J Control Release 163:293\u2013303. https:\/\/doi.org\/10.1016\/j.jconrel.2012.09.019","journal-title":"J Control Release"},{"key":"4618_CR52","doi-asserted-by":"publisher","first-page":"691532","DOI":"10.3389\/fchem.2021.691532","volume":"9","author":"T Sarkar","year":"2021","unstructured":"Sarkar T, Chetia M, Chatterjee S (2021) Antimicrobial peptides and proteins: from nature\u2019s reservoir to the laboratory and beyond. Front Chem 9:691532. https:\/\/doi.org\/10.3389\/fchem.2021.691532","journal-title":"Front Chem"},{"issue":"1","key":"4618_CR53","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1038\/nprot.2006.4","volume":"1","author":"H Sch\u00e4gger","year":"2006","unstructured":"Sch\u00e4gger H (2006) Tricine-SDS-PAGE. Nat Protoc 1(1):16\u201322","journal-title":"Nat Protoc"},{"issue":"4","key":"4618_CR54","doi-asserted-by":"publisher","first-page":"2005","DOI":"10.1128\/iai.67.4.2005-2009.1999","volume":"67","author":"MG Scott","year":"1999","unstructured":"Scott MG, Yan H, Hancock RE (1999) Biological properties of structurally related \u03b1-helical cationic antimicrobial peptides. Infect Immun 67(4):2005\u20132009. https:\/\/doi.org\/10.1128\/iai.67.4.2005-2009.1999","journal-title":"Infect Immun"},{"issue":"1","key":"4618_CR55","doi-asserted-by":"publisher","first-page":"64","DOI":"10.1093\/biohorizons\/hzp001","volume":"2","author":"V Sebbage","year":"2009","unstructured":"Sebbage V (2009) Cell-penetrating peptides and their therapeutic applications. Biosci Horiz 2(1):64\u201372. https:\/\/doi.org\/10.1093\/biohorizons\/hzp001","journal-title":"Biosci Horiz"},{"issue":"6","key":"4618_CR56","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1038\/ni1206","volume":"6","author":"ME Selsted","year":"2005","unstructured":"Selsted ME, Ouellette AJ (2005) Mammalian defensins in the antimicrobial immune response. Nat Immunol 6(6):551\u2013557. https:\/\/doi.org\/10.1038\/ni1206","journal-title":"Nat Immunol"},{"key":"4618_CR57","doi-asserted-by":"publisher","first-page":"104930","DOI":"10.1016\/j.micpath.2021.104930","volume":"155","author":"SS Solanki","year":"2021","unstructured":"Solanki SS, Singh P, Kashyap P, Sansi MS, Ali SA (2021) Promising role of defensins peptides as therapeutics to combat against viral infection. Microb Pathog 155:104930. https:\/\/doi.org\/10.1016\/j.micpath.2021.104930","journal-title":"Microb Pathog"},{"key":"4618_CR58","doi-asserted-by":"publisher","first-page":"60","DOI":"10.1186\/s40104-019-0367-0","volume":"10","author":"G Su","year":"2019","unstructured":"Su G, Xie K, Chen D, Yu B, Huang Z, Luo Y, Mao X, Zheng P, Yu J, Luo J, He J (2019) Differential expression, molecular cloning, and characterization of Porcine beta defensin 114. J Anim Sci Biotechnol 10:60. https:\/\/doi.org\/10.1186\/s40104-019-0367-0","journal-title":"J Anim Sci Biotechnol"},{"issue":"1","key":"4618_CR59","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1034\/j.1399-3011.2001.00800.x","volume":"57","author":"C Subbalakshmi","year":"2001","unstructured":"Subbalakshmi C, Nagaraj R, Sitaram N (2001) Biological activities of retro and diastereo analogs of a 13-residue peptide with antimicrobial and hemolytic activities. J Pept Res 57(1):59\u201367. https:\/\/doi.org\/10.1034\/j.1399-3011.2001.00800.x","journal-title":"J Pept Res"},{"key":"4618_CR60","doi-asserted-by":"publisher","unstructured":"Tao K, He C, Zhu Y, Li Z, Shao D, Li B, \u2026 and, Liu K (2025) The other side of defensins: review of antiviral activity of defensins. Appl Biochem Microbiol 1\u201312. https:\/\/doi.org\/10.1134\/S0003683824608382","DOI":"10.1134\/S0003683824608382"},{"issue":"45","key":"4618_CR61","doi-asserted-by":"publisher","first-page":"10686","DOI":"10.1002\/anie.201103589","volume":"50","author":"M Torrent","year":"2011","unstructured":"Torrent M, Valle J, Nogu\u00e9s MV, Boix E, Andreu D (2011) The generation of antimicrobial peptide activity: a trade-off between charge and aggregation? Angewandte Chemie-International Ed 50(45):10686. https:\/\/doi.org\/10.1002\/anie.201103589","journal-title":"Angewandte Chemie-International Ed"},{"issue":"18","key":"4618_CR62","doi-asserted-by":"publisher","first-page":"3547","DOI":"10.1016\/j.jmb.2018.12.015","volume":"431","author":"MD Torres","year":"2019","unstructured":"Torres MD, Sothiselvam S, Lu TK, de la Fuente-Nunez C (2019) Peptide design principles for antimicrobial applications. J Mol Biol 431(18):3547\u20133567. https:\/\/doi.org\/10.1016\/j.jmb.2018.12.015","journal-title":"J Mol Biol"},{"key":"4618_CR63","doi-asserted-by":"publisher","first-page":"764","DOI":"10.3389\/fimmu.2020.00764","volume":"11","author":"D Xu","year":"2020","unstructured":"Xu D, Lu W (2020) Defensins: a double-edged sword in host immunity. Front Immunol 11:764. https:\/\/doi.org\/10.3389\/fimmu.2020.00764","journal-title":"Front Immunol"},{"issue":"6","key":"4618_CR64","doi-asserted-by":"publisher","first-page":"e98935","DOI":"10.1371\/journal.pone.0098935","volume":"9","author":"W Xu","year":"2014","unstructured":"Xu W, Zhu X, Tan T, Li W, Shan A (2014) Design of Embedded-Hybrid antimicrobial peptides with enhanced cell selectivity and Anti-Biofilm activity. PLoS ONE 9(6):e98935. https:\/\/doi.org\/10.1371\/journal.pone.0098935","journal-title":"PLoS ONE"},{"issue":"7","key":"4618_CR65","doi-asserted-by":"publisher","first-page":"1289","DOI":"10.1039\/C4CC08808E","volume":"51","author":"D Xu","year":"2015","unstructured":"Xu D, Jiang L, Singh A, Dustin D, Yang M, Liu L, Lund R, Sellati TJ, Dong H (2015) Designed supramolecular filamentous cationic peptides: balance of Nanostructure, cytotoxicity and antimicrobial activity. Chem Commun 51(7):1289\u20131292. https:\/\/doi.org\/10.1039\/C4CC08808E","journal-title":"Chem Commun"},{"key":"4618_CR66","doi-asserted-by":"publisher","first-page":"448","DOI":"10.1189\/jlb.0103024","volume":"74","author":"D Yang","year":"2003","unstructured":"Yang D, Chen Q, Hoover DM, Staley P, Tucker KD, Lubkowski J (2003) Many chemokines including CCL20\/MIP-3alpha display antimicrobial activity. J Leukoc Biol 74:448\u2013455. https:\/\/doi.org\/10.1189\/jlb.0103024","journal-title":"J Leukoc Biol"},{"issue":"10","key":"4618_CR67","doi-asserted-by":"publisher","first-page":"4918","DOI":"10.1128\/aac.00202-11","volume":"55","author":"HY Yu","year":"2011","unstructured":"Yu HY, Tu CH, Yip BS, Chen HL, Cheng HT, Huang KC, Lo HJ, Cheng JW (2011) Easy strategy to increase salt resistance of antimicrobial peptides. Antimicrob Agents Chemother 55(10):4918\u20134921. https:\/\/doi.org\/10.1128\/aac.00202-11","journal-title":"Antimicrob Agents Chemother"},{"issue":"2","key":"4618_CR68","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1016\/j.pep.2011.04.013","volume":"78","author":"J Zhang","year":"2011","unstructured":"Zhang J, Yang Y, Teng D, Tian Z, Wang S, Wang J (2011) Expression of plectasin in Pichia pastoris and its characterization as a new antimicrobial peptide against Staphyloccocus and Streptococcus. Protein Expr Purif 78(2):189\u2013196. https:\/\/doi.org\/10.1016\/j.pep.2011.04.013","journal-title":"Protein Expr Purif"},{"key":"4618_CR69","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1016\/j.jconrel.2016.03.020","volume":"229","author":"D Zhang","year":"2016","unstructured":"Zhang D, Wang J, Xu D (2016) Cell-penetrating peptides as noninvasive transmembrane vectors for the development of novel multifunctional drug-delivery systems. J Control Release 229:130\u2013139. https:\/\/doi.org\/10.1016\/j.jconrel.2016.03.020","journal-title":"J Control Release"}],"updated-by":[{"DOI":"10.1007\/s11274-025-04745-5","type":"correction","label":"Correction","source":"publisher","updated":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T00:00:00Z","timestamp":1773187200000}}],"container-title":["World Journal of Microbiology and Biotechnology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11274-025-04618-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11274-025-04618-x","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11274-025-04618-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T06:27:07Z","timestamp":1773210427000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11274-025-04618-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,10]]},"references-count":69,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2025,10]]}},"alternative-id":["4618"],"URL":"https:\/\/doi.org\/10.1007\/s11274-025-04618-x","relation":{},"ISSN":["0959-3993","1573-0972"],"issn-type":[{"value":"0959-3993","type":"print"},{"value":"1573-0972","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,10]]},"assertion":[{"value":"25 February 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"26 September 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"16 October 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 March 2026","order":5,"name":"change_date","label":"Change Date","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Correction","order":6,"name":"change_type","label":"Change Type","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"A Correction to this paper has been published:","order":7,"name":"change_details","label":"Change Details","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"https:\/\/doi.org\/10.1007\/s11274-025-04745-5","URL":"https:\/\/doi.org\/10.1007\/s11274-025-04745-5","order":8,"name":"change_details","label":"Change Details","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Due to the scope of the study, there was an ethics committee permission document for hemolytic activity assay. The ethics committee\u2019s permission was obtained from Erciyes University Local Ethics Committee for Animal Experiments (HADYEK), and the permission number was 22\/110-01\/06\/2022.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical approval"}},{"value":"The authors declare no competing interests.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"392"}}