{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T06:46:55Z","timestamp":1788245215958,"version":"build-2803163510"},"reference-count":55,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2017,3,12]],"date-time":"2017-03-12T00:00:00Z","timestamp":1489276800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Linear, dimeric, tetrameric, and cyclic peptides derived from lactoferricin B\u2013containing non-natural amino acids and the RWQWR motif were synthesized, purified, and characterized using RP-HPLC, MALDI-TOF mass spectrometry, and circular dichroism. The antibacterial activity of peptides against Escherichia coli ATCC 11775, Stenotrophomonas maltophilia ATCC 13636, and Salmonella enteritidis ATCC 13076 was evaluated. The minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) were determined. The synthetic bovine lactoferricin exhibited antibacterial activity against E. coli ATCC 11775 and S. enteritidis ATCC 13076. The dimeric peptide (RRWQWR)2K-Ahx exhibited the highest antibacterial activity against the tested bacterial strain. The monomeric, cyclic, tetrameric, and palindromic peptides containing the RWQWR motif exhibited high and specific activity against E. coli ATCC 11775. The results suggest that short peptides derived from lactoferricin B could be considered as potential candidates for the development of antibacterial agents against infections caused by E. coli.<\/jats:p>","DOI":"10.3390\/molecules22030452","type":"journal-article","created":{"date-parts":[[2017,3,13]],"date-time":"2017-03-13T10:26:18Z","timestamp":1489400778000},"page":"452","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":46,"title":["Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Antimicrobial Activity against E. coli ATCC 11775, S. maltophilia ATCC 13636 and S. enteritidis ATCC 13076"],"prefix":"10.3390","volume":"22","author":[{"given":"Nataly","family":"Huertas M\u00e9ndez","sequence":"first","affiliation":[{"name":"Chemistry Department, Universidad Nacional de Colombia, Bogot\u00e1 Carrera 45 No 26-85, Building 451, office 409, Bogot\u00e1 11321, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yerly","family":"Vargas Casanova","sequence":"additional","affiliation":[{"name":"Bacteriology Department, Universidad Colegio Mayor de Cundinamarca, Bogot\u00e1 Calle 28 No. 5B-02, Bogot\u00e1 110311; Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anyelith","family":"G\u00f3mez Chimbi","sequence":"additional","affiliation":[{"name":"Bacteriology Department, Universidad Colegio Mayor de Cundinamarca, Bogot\u00e1 Calle 28 No. 5B-02, Bogot\u00e1 110311; Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edith","family":"Hern\u00e1ndez","sequence":"additional","affiliation":[{"name":"Bacteriology Department, Universidad Colegio Mayor de Cundinamarca, Bogot\u00e1 Calle 28 No. 5B-02, Bogot\u00e1 110311; Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aura","family":"Leal Castro","sequence":"additional","affiliation":[{"name":"Medicine Faculty, Universidad Nacional de Colombia, Bogot\u00e1 Carrera 45 No 26-85, Building 471, Bogot\u00e1 11321, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Javier","family":"Melo Diaz","sequence":"additional","affiliation":[{"name":"Chemistry Department, Universidad Nacional de Colombia, Bogot\u00e1 Carrera 45 No 26-85, Building 451, office 409, Bogot\u00e1 11321, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zuly","family":"Rivera Monroy","sequence":"additional","affiliation":[{"name":"Chemistry Department, Universidad Nacional de Colombia, Bogot\u00e1 Carrera 45 No 26-85, Building 451, office 409, Bogot\u00e1 11321, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6882-4397","authenticated-orcid":false,"given":"Javier","family":"Garc\u00eda Casta\u00f1eda","sequence":"additional","affiliation":[{"name":"Pharmacy Department, Universidad Nacional de Colombia, Bogot\u00e1 Carrera 45 No 26-85, Building 450, office 203, Bogot\u00e1 11321, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2017,3,12]]},"reference":[{"key":"ref_1","unstructured":"World Health Organization Antimicrobial Resistance, Global Report on Surveillance. Available online: http:\/\/apps.who.int\/iris\/bitstream\/10665\/112642\/1\/9789241564748_eng.pdf?ua=1."},{"key":"ref_2","unstructured":"Gelband, H., Miller-Petrie, M., Pant, S., Gandra, S., Levinson, J., Barter, D., White, A., and Laxminarayan, R. (2015). State of the World\u2019s Antibiotics, Center for Disease Dynamics, Economics & Policy (CDDEP)."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1128\/CMR.00019-11","article-title":"Stenotrophomonas maltophilia: An Emerging Global Opportunistic Pathogen","volume":"25","author":"Brooke","year":"2012","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1186\/1476-0711-5-23","article-title":"Case report. Stenotrophomonas maltophilia resistant to trimethoprim - sulfamethoxazole: An increasing problem.","volume":"5","year":"2006","journal-title":"Ann. Clin. Microb. Antimicrob."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1128\/AAC.44.2.287-293.2000","article-title":"Multiple Antibiotic Resistance in Stenotrophomonas maltophilia: Involvement of a Multidrug Efflux System","volume":"44","author":"Zhang","year":"2000","journal-title":"Antimicrob. Agents. Chemother."},{"key":"ref_6","unstructured":"World Health Organization Antimicrobial resistance. Available online: http:\/\/www.who.int\/mediacentre\/factsheets\/fs139\/en\/."},{"key":"ref_7","first-page":"9","article-title":"Microbial-resistant Salmonella enteritidis isolated from poultry samples","volume":"1","author":"Ghazaey","year":"2012","journal-title":"Rep. Biochem. Mol. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.drudis.2009.10.009","article-title":"Synthetic therapeutic peptides: Science and market","volume":"15","author":"Vlieghe","year":"2010","journal-title":"Drug. Discov. Today"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.euprot.2014.05.003","article-title":"The emergence of peptides in the pharmaceutical business: From exploration to exploitation","volume":"4","author":"Uhlig","year":"2014","journal-title":"EuPA Open Proteom."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/j.ijantimicag.2004.09.005","article-title":"Antimicrobial peptides: Premises and promises","volume":"24","author":"Reddy","year":"2004","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.3390\/ph6121543","article-title":"Antimicrobial Peptides","volume":"6","author":"Bahar","year":"2013","journal-title":"Pharmaceuticals"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/S0161-5890(03)00152-4","article-title":"Lactoferrin a multifunctional protein with antimicrobial properties","volume":"40","author":"Farnaud","year":"2003","journal-title":"Mol. Immunol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1146\/annurev.nu.15.070195.000521","article-title":"Lactoferrin: Molecular structure and biological function","volume":"15","author":"Lonnerdal","year":"1995","journal-title":"Annu. Rev. Nutr."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.bbagen.2011.06.018","article-title":"Lactoferrin a multiple bioactive protein: An overview","volume":"1820","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.biochi.2008.05.021","article-title":"Twenty-five years of research on bovine lactoferrin applications","volume":"91","author":"Tomita","year":"2009","journal-title":"Biochimie"},{"key":"ref_16","first-page":"472","article-title":"Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin","volume":"73","author":"Bellamy","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1128\/iai.28.3.893-898.1980","article-title":"Bactericidal activity of human lactoferrin: Sensitivity of a variety of microorganisms","volume":"28","author":"Arnold","year":"1980","journal-title":"Infect. Immun."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1953","DOI":"10.1016\/j.peptides.2011.07.017","article-title":"Discovery and development of a synthetic peptide derived from lactoferrin for clinical use","volume":"32","author":"Brouwer","year":"2011","journal-title":"Peptides"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1021\/jm0340039","article-title":"The Pharmacophore of Short Cationic Antibacterial Peptides","volume":"46","author":"Haug","year":"2003","journal-title":"J. Med. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/0167-4838(92)90346-F","article-title":"Identification of the bactericidal domain of lactoferrin","volume":"1121","author":"Bellamy","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2013\/390230","article-title":"Antimicrobial Lactoferrin Peptides: The Hidden Players in the Protective Function of a Multifunctional Protein","volume":"2013","author":"Sinha","year":"2013","journal-title":"Int. J. Pep."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/S0014-5793(01)02233-5","article-title":"Lactoferricin B causes depolarization of the cytoplasmic membrane of Escherichia coli ATCC 25922 and fusion of negatively charged liposomes","volume":"492","author":"Ulvatne","year":"2001","journal-title":"FEBS Lett."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0166-3542(01)00146-2","article-title":"Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomegalovirus into human fibroblasts","volume":"51","author":"Andersen","year":"2001","journal-title":"Antiviral Res."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0166-3542(02)00214-0","article-title":"Lactoferrin and lactoferricin inhibit Herpes simplex 1 and 2 infection and exhibit synergy when combined with acyclovir","volume":"58","author":"Andersen","year":"2003","journal-title":"Antiviral Res."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/S0014-5793(99)01545-8","article-title":"Permeabilizing action of an antimicrobial lactoferricin-derived peptide on bacterial and artificial membranes","volume":"462","author":"Aguilera","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.1016\/j.bbamem.2006.04.006","article-title":"Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action","volume":"1758","author":"Chan","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/S0014-5793(01)03100-3","article-title":"The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm","volume":"508","author":"Haukland","year":"2001","journal-title":"FEBS Lett."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1007\/s10534-011-9465-y","article-title":"Comparative antimicrobial activity and mechanism of action of bovine lactoferricin-derived synthetic peptides","volume":"24","author":"Liu","year":"2011","journal-title":"Biometals"},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Tu, Y.H., Ho, Y.h., Chuang, Y.C., Chen, P.C., and Chen, C.S. (2011). Identification of Lactoferricin B Intracellular Targets Using an Escherichia coli Proteome Chip. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0028197"},{"key":"ref_30","first-page":"377","article-title":"Lactoferricin B inhibits bacterial macromolecular synthesis in Escherichia coli and Bacillus subtilis","volume":"15","author":"Ulvatne","year":"2004","journal-title":"FEMS. Microbiol. Lett."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1080\/00365549850161557","article-title":"Lactoferricin of bovine origin is more active than lactoferricins of human, murine and caprine origin","volume":"30","author":"Vorland","year":"1998","journal-title":"Scand. J. Infect. Dis."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0014-5793(99)00214-8","article-title":"The structure of the antimicrobial active center of lactoferricin B bound to sodium dodecyl sulfate micelles","volume":"446","author":"Schibli","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1002\/psc.1047","article-title":"Lipid interactions of acylated tryptophan-methylated lactoferricin peptides by solid-state NMR","volume":"14","author":"Greathouse","year":"2008","journal-title":"J. Pept. Sci."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Nguyen, L.T., Chau, J.K., Perry, N.A., de Boer, L., Zaat, S.A., and Vogel, H.J. (2010). Serum stabilities of short tryptophan- and arginine-rich antimicrobial peptide analogs. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0012684"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1111\/febs.12093","article-title":"The six amino acid antimicrobial peptide bLFcin6 penetrates cells and delivers siRNA","volume":"280","author":"Fang","year":"2013","journal-title":"FEBS J."},{"key":"ref_36","first-page":"1","article-title":"Antibacterial activity of synthetic peptides derived from Lactoferricin against Escherichia coli ATCC 25922 and Enterococcus faecalis ATCC 29212","volume":"2015","author":"Leal","year":"2015","journal-title":"Biomed. Res. Int."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1002\/(SICI)1099-1387(199901)5:1<32::AID-PSC172>3.0.CO;2-9","article-title":"Construction and synthesis of lactoferricin derivatives with enhanced antibacterial activity","volume":"5","author":"Rekdal","year":"1999","journal-title":"J. Pept. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1002\/psc.338","article-title":"Bulky aromatic amino acids increase the antibacterial activity of 15-residue bovine lactoferricin derivatives","volume":"7","author":"Haug","year":"2001","journal-title":"J. Pept. Sci."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1267","DOI":"10.1128\/AAC.43.5.1267","article-title":"N-Acylated and D enantiomer derivatives of a nonamer core peptide of lactoferricin B showing improved antimicrobial activity","volume":"43","author":"Wakabayashi","year":"1999","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1128\/AAC.41.1.54","article-title":"Antibacterial activity in bovine lactoferrin-derived peptides","volume":"41","author":"Hoek","year":"1997","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1124\/jpet.109.162826","article-title":"Metabolic fate of lactoferricin-based antimicrobial peptides: Effect of truncation and incorporation of amino acid analogs on the in vitro metabolic stability","volume":"332","author":"Svenson","year":"2010","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1034\/j.1399-3011.2000.00770.x","article-title":"Antibacterial activity of 15-residue lactoferricin derivatives","volume":"56","author":"Rekdal","year":"2000","journal-title":"J. Pept. Res."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.2460\/ajvr.2003.64.1088","article-title":"Antibacterial activity of short hydrophobic and basic rich peptides","volume":"64","author":"Chen","year":"2003","journal-title":"Am. J. Vet. Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1515\/BC.2008.116","article-title":"Conformational changes in bovine lactoferrin induced by slow or fast temperature increases","volume":"389","author":"Schwarcz","year":"2008","journal-title":"Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1080\/003655499750006245","article-title":"Antibacterial effects of lactoferricin B","volume":"31","author":"Vorland","year":"1999","journal-title":"Scand. J. Infect. Dis."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1093\/jac\/dkq106","article-title":"Evaluation of synergistic activity of bovine lactoferricin with antibiotics in corneal infection","volume":"65","author":"Oo","year":"2010","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_47","unstructured":"MilkAMP database A database dedicated to milk antimicrobial peptides. Available online: http:\/\/milkampdb.org\/BLF0084."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1128\/iai.61.2.719-728.1993","article-title":"Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment","volume":"61","author":"Yamauchi","year":"1993","journal-title":"Infect. Immun."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1093\/jac\/dkf156","article-title":"Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B","volume":"50","author":"Ulvatne","year":"2002","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2019","DOI":"10.1016\/j.bbamem.2011.03.017","article-title":"Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations","volume":"1808","author":"Romo","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1046\/j.1472-765x.2000.00711.x","article-title":"Activity of hydrolysed lactoferrin against foodborne pathogenic bacteria in growth media: The effect of EDTA","volume":"30","author":"Branen","year":"2000","journal-title":"Lett. Appl. Microbiol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"4425","DOI":"10.1128\/AAC.49.10.4425-4426.2005","article-title":"Antibiotic susceptibility of Stenotrophomonas maltophilia in the presence of Lactoferrin","volume":"49","author":"Qamruddin","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_53","first-page":"386","article-title":"Efficient Synthesis of Peptides with 4-Methylpiperidine as Fmoc Removal Reagent by Solid Phase Synthesis","volume":"58","author":"Vergel","year":"2014","journal-title":"J. Mex. Chem. Soc."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.bbrc.2007.01.167","article-title":"Monosacharides modulate HCV E2 Protein-derived peptide biological properties","volume":"355","author":"Fierro","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"630179","DOI":"10.1155\/2015\/630179","article-title":"A Tetrameric Peptide Derived from Bovine Lactoferricin Exhibits Specific Cytotoxic Effects against Oral Squamous-Cell Carcinoma Cell Lines","volume":"2015","author":"Solarte","year":"2015","journal-title":"Biomed. Res. Int."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/22\/3\/452\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T18:30:17Z","timestamp":1760207417000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/22\/3\/452"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,3,12]]},"references-count":55,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2017,3]]}},"alternative-id":["molecules22030452"],"URL":"https:\/\/doi.org\/10.3390\/molecules22030452","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,3,12]]}}}