{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T22:40:24Z","timestamp":1787784024047,"version":"build-2784847793"},"reference-count":33,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2022,11,7]],"date-time":"2022-11-07T00:00:00Z","timestamp":1667779200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Universidad Colegio Mayor de Cundinamarca","award":["112\/2017"],"award-info":[{"award-number":["112\/2017"]}]},{"name":"School of Medicine and Health Sciences, Universidad del Rosario","award":["112\/2017"],"award-info":[{"award-number":["112\/2017"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JoF"],"abstract":"<jats:p>Fungal infections have increased in recent decades with considerable morbidity and mortality, mainly in immunosuppressed or admitted-to-the-ICU patients. The fungal resistance to conventional antifungal treatments has become a public health problem, especially with Candida that presents resistance to several antifungals. Therefore, generating new alternatives of antifungal therapy is fundamental. One of these possibilities is the use of antimicrobial peptides, such as LL-37, which acts on the disruption of the microorganism membrane and promotes immunomodulatory effects in the host. In this study, we evaluated the in vitro antifungal activity of the LL-37 analogue peptides (AC-1, LL37-1, AC-2, and D) against different Candida spp. and clinical isolates obtained from patients with vulvovaginal candidiasis. Our results suggest that the peptides with the best ranges of MICs were LL37-1 and AC-2 (0.07 \u00b5M) against the strains studied. This inhibitory effect was confirmed by analyzing the yeast growth curves that evidenced a significant decrease in the fungal growth after exposure to LL-37 peptides. By the XTT technique we observed a significant reduction in the biofilm formation process when compared to yeasts untreated with the analogue peptides. In conclusion, we suggest that LL-37 analogue peptides may play an important antimicrobial role against Candida spp.<\/jats:p>","DOI":"10.3390\/jof8111173","type":"journal-article","created":{"date-parts":[[2022,11,8]],"date-time":"2022-11-08T10:53:52Z","timestamp":1667904832000},"page":"1173","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["In Vitro Antifungal Activity of LL-37 Analogue Peptides against Candida spp."],"prefix":"10.3390","volume":"8","author":[{"given":"Gladys","family":"Pinilla","sequence":"first","affiliation":[{"name":"Grupo de Investigaci\u00f3n REMA, Faculty of Health Sciences, Universidad Colegio Mayor de Cundinamarca, Calle 28 # 5-B-02, Bogot\u00e1 110311, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yenifer Tatiana","family":"Coronado","sequence":"additional","affiliation":[{"name":"Grupo de Investigaci\u00f3n REMA, Faculty of Health Sciences, Universidad Colegio Mayor de Cundinamarca, Calle 28 # 5-B-02, Bogot\u00e1 110311, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gabriel","family":"Chaves","sequence":"additional","affiliation":[{"name":"Grupo de Investigaci\u00f3n REMA, Faculty of Health Sciences, Universidad Colegio Mayor de Cundinamarca, Calle 28 # 5-B-02, Bogot\u00e1 110311, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liliana","family":"Mu\u00f1oz","sequence":"additional","affiliation":[{"name":"Grupo de Investigaci\u00f3n REMA, Faculty of Health Sciences, Universidad Colegio Mayor de Cundinamarca, Calle 28 # 5-B-02, Bogot\u00e1 110311, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeannette","family":"Navarrete","sequence":"additional","affiliation":[{"name":"Grupo de Investigaci\u00f3n REMA, Faculty of Health Sciences, Universidad Colegio Mayor de Cundinamarca, Calle 28 # 5-B-02, Bogot\u00e1 110311, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luz Mary","family":"Salazar","sequence":"additional","affiliation":[{"name":"Departamento de Qu\u00edmica, Facultad de Ciencias, Universidad Nacional de Colombia, Carrera 30 # 45-03, Ciudad Universitaria, Bogot\u00e1 111321, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9928-9809","authenticated-orcid":false,"given":"Carlos Pelleschi","family":"Taborda","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Biomedical Sciences Institute, University of S\u00e3o Paulo, S\u00e3o Paulo 05508-000, Brazil"},{"name":"Laboratory of Medical Mycology, Institute of Tropical Medicine of S\u00e3o Paulo LIM53\/Medical School, University of S\u00e3o Paulo, S\u00e3o Paulo 4023-062, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4495-7077","authenticated-orcid":false,"given":"Juli\u00e1n E.","family":"Mu\u00f1oz","sequence":"additional","affiliation":[{"name":"Studies in Translational Microbiology and Emerging Diseases (MICROS) Research Group, Translational Medicine Institute, School of Medicine and Health Sciences, Universidad del Rosario, Calle 63 C # 26-63, Bogot\u00e1 111221, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,11,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S0123-9392(10)70133-8","article-title":"Candida y candidiasis invasora: Un reto continuo para su diagn\u00f3stico temprano","volume":"14","year":"2010","journal-title":"Infectio"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"18026","DOI":"10.1038\/nrdp.2018.26","article-title":"Invasive candidiasis","volume":"4","author":"Pappas","year":"2018","journal-title":"Nat. Rev. Dis. Prim."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Alvarez-Moreno, C.A., Cortes, J.A., and Denning, D.W. (2018). Burden of fungal infections in Colombia. J. Fungi, 4.","DOI":"10.3390\/jof4020041"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1128\/JCM.01398-10","article-title":"Geographic variations in species distribution and echinocandin and azole antifungal resistance rates among Candida bloodstream infection isolates: Report from the SENTRY Antimicrobial Surveillance Program (2008 to 2009)","volume":"49","author":"Pfaller","year":"2011","journal-title":"J. Clin. Microbiol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"105","DOI":"10.3389\/fcimb.2020.00105","article-title":"Antifungal Peptides as Therapeutic Agents","volume":"10","author":"Arbulu","year":"2020","journal-title":"Front. Cell Infect Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1007\/s10529-005-0936-5","article-title":"Human antimicrobial peptides: Defensins, cathelicidins and histatins","volume":"27","author":"Contreras","year":"2005","journal-title":"Biotechnol. Lett."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1408","DOI":"10.1016\/j.bbamem.2006.03.030","article-title":"LL-37, the only human member of the cathelicidin family of antimicrobial peptides","volume":"1758","author":"Sudheendra","year":"2006","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"143","DOI":"10.3389\/fimmu.2013.00143","article-title":"The human cathelicidin antimicrobial peptide LL-37 as a potential treatment for polymicrobial infected wounds","volume":"4","author":"Duplantier","year":"2013","journal-title":"Front. Immunol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"e3254","DOI":"10.1002\/psc.3254","article-title":"Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial\/anticancer agents","volume":"26","author":"Tzitzilis","year":"2020","journal-title":"J. Pept. Sci."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1080\/02713680590934111","article-title":"Human cathelicidin (LL-37), a multifunctional peptide, is expressed by ocular surface epithelia and has potent antibacterial and antiviral activity","volume":"30","author":"Gordon","year":"2005","journal-title":"Curr. Eye Res."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Tsai, P., Yang, C., Chang, H., and Lan, C. (2011). Human Antimicrobial Peptide LL-37 Inhibits Adhesion of Candida albicans by Interacting with Yeast Cell-Wall Carbohydrates. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0017755"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2697","DOI":"10.3389\/fimmu.2019.02697","article-title":"Cathelicidin Contributes to the Restriction of Leishmania in Human Host Macrophages","volume":"10","author":"Crauwels","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.cellimm.2012.11.009","article-title":"A comprehensive summary of LL-37, the factoctum human cathelicidin peptide","volume":"280","author":"Vandamme","year":"2012","journal-title":"Cell Immunol."},{"key":"ref_14","first-page":"62","article-title":"P\u00e9ptidos antimicrobianos en la inmunidad innata de enfermedades infecciosas","volume":"48","author":"Sada","year":"2006","journal-title":"Salud Publica Mex."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"3086","DOI":"10.1182\/blood.V96.9.3086","article-title":"The human antimicrobial and chemotactic peptides LL-37 and \u03b1-defensins are expressed by specific lymphocyte and monocyte populations","volume":"96","author":"Agerberth","year":"2000","journal-title":"Blood"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1776","DOI":"10.4049\/jimmunol.175.3.1776","article-title":"The Human \u03b2-Defensins (-1, -2, -3, -4) and Cathelicidin LL-37 Induce IL-18 Secretion through p38 and ERK MAPK Activation in Primary Human Keratinocytes","volume":"175","author":"Niyonsaba","year":"2005","journal-title":"J. Immunol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/j.exppara.2012.12.009","article-title":"Effect of antimicrobial peptides derived from human cathelicidin LL-37 on Entamoeba histolytica trophozoites","volume":"133","author":"Avila","year":"2013","journal-title":"Exp. Parasitol."},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Nguyen, L.T., Chau, J.K., Perry, N.A., de Boer, L., Zaat, S.A.J., 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_19","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.1038\/nprot.2008.141","article-title":"A simple and reproducible 96 well plate-based methos for the formation of fungal biofilms and its application to antifungal susceptibility testing","volume":"3","author":"Pierce","year":"2008","journal-title":"Nat. Protoc."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.pharmthera.2017.04.002","article-title":"Antimicrobial peptides: Role in human disease and potential as immunotherapies","volume":"178","author":"Silva","year":"2017","journal-title":"Pharmacol. Ther."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"16","DOI":"10.2174\/1568026615666150703121518","article-title":"Interactions of Antimicrobial Peptides with Bacterial Membranes and Membrane Components","volume":"16","author":"Malmsten","year":"2016","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1016\/j.febslet.2013.01.026","article-title":"Effect of amino acid distribution of amphipathic helical peptide derived from human apolipoprotein A-I on membrane curvature sensing","volume":"587","author":"Tanaka","year":"2013","journal-title":"FEBS Lett."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1016\/j.colsurfb.2016.02.003","article-title":"Role of amphipathicity and hydrophobicity in the balance between hemolysis and peptide-membrane interactions of three related antimicrobial peptides","volume":"141","author":"Hollmann","year":"2016","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1016\/j.bbamem.2017.12.018","article-title":"Effect of N-terminal acetylation on lytic activity and lipid-packing perturbation induced in model membranes by a mastoparan-like peptide","volume":"1860","author":"Alvares","year":"2018","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1007\/s12275-014-3630-2","article-title":"Responses of Candida albicans to the Human Antimicrobial Peptide LL-37","volume":"52","author":"Tsai","year":"2014","journal-title":"J. Microbiol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"3777","DOI":"10.1016\/j.tetlet.2012.05.039","article-title":"Enzymatic C-terminal amidation of amino acids and peptides","volume":"53","author":"Nuijens","year":"2012","journal-title":"Tetrahedron Lett."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1851","DOI":"10.1016\/j.bbamem.2017.06.005","article-title":"Synthetic antimicrobial peptides of the halictines family disturb the membrane integrity of Candida cells","volume":"1859","year":"2017","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Pierce, C.G., Vila, T., Romo, J.A., Montelongo-Jauregui, D., Wall, G., Ramasubramanian, A., and Lopez-Ribot, J.L. (2017). The Candida albicans biofilm matrix: Composition, structure and function. J. Fungi., 3.","DOI":"10.3390\/jof3010014"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"28","DOI":"10.3389\/fmed.2018.00028","article-title":"Candida Biofilms: Threats, challenges, and promising strategies","volume":"5","author":"Cavalheiro","year":"2018","journal-title":"Front. Med."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"35018","DOI":"10.1038\/srep35018","article-title":"A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents","volume":"6","author":"Polonelli","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Ridyard, K.E., and Overhage, J. (2021). The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent. Antibiotics, 10.","DOI":"10.3390\/antibiotics10060650"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Le\u00f3n-Buitimea, A., Garza-Cervantes, J.A., Gallegos-Alvarado, D.Y., Osorio-Concepci\u00f3n, M., and Morones-Ram\u00edrez, J.R. (2021). Nanomaterial-based antifungal therapies to combat fungal diseases aspergillosis, coccidioidomycosis, mucormycosis, and candidiasis. Pathogens, 10.","DOI":"10.3390\/pathogens10101303"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.colsurfb.2012.06.005","article-title":"Size and shape dependant antifungal activity of gold nanoparticles: A case study of Candida","volume":"101","author":"Wani","year":"2013","journal-title":"Colloids Surf. Biointerfaces"}],"container-title":["Journal of Fungi"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2309-608X\/8\/11\/1173\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T01:11:53Z","timestamp":1760145113000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2309-608X\/8\/11\/1173"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,11,7]]},"references-count":33,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2022,11]]}},"alternative-id":["jof8111173"],"URL":"https:\/\/doi.org\/10.3390\/jof8111173","relation":{},"ISSN":["2309-608X"],"issn-type":[{"value":"2309-608X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,11,7]]}}}