Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against <i>Staphylococcus aureus</i>, <i>Escherichia coli</i>, and <i>Candida albicans</i>
Various peptides and their derivatives have been reported to exhibit antimicrobial activities. Although these activities have been examined against microorganisms, novel methods have recently emerged for conjugation of the biomaterials to improve their activities. Here, we prepared CKR12-PLGA, in wh...
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| Format: | Article |
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MDPI AG
2021-05-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/10/5097 |
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| author | Takeshi Mori Miyako Yoshida Mai Hazekawa Daisuke Ishibashi Yoshiro Hatanaka Toshihiro Nagao Rie Kakehashi Honami Kojima Rio Uno Minoru Ozeki Ikuo Kawasaki Taku Yamashita Junichi Nishikawa Takahiro Uchida |
| author_facet | Takeshi Mori Miyako Yoshida Mai Hazekawa Daisuke Ishibashi Yoshiro Hatanaka Toshihiro Nagao Rie Kakehashi Honami Kojima Rio Uno Minoru Ozeki Ikuo Kawasaki Taku Yamashita Junichi Nishikawa Takahiro Uchida |
| author_sort | Takeshi Mori |
| collection | DOAJ |
| description | Various peptides and their derivatives have been reported to exhibit antimicrobial activities. Although these activities have been examined against microorganisms, novel methods have recently emerged for conjugation of the biomaterials to improve their activities. Here, we prepared CKR12-PLGA, in which CKR12 (a mutated fragment of human cathelicidin peptide, LL-37) was conjugated with poly (lactic-co-glycolic) acid (PLGA), and compared the antimicrobial and antifungal activities of the conjugated peptide with those of FK13 (a small fragment of LL-37) and CKR12 alone. The prepared CKR12-PLGA was characterized by dynamic light scattering and measurement of the zeta potential, critical micellar concentration, and antimicrobial activities of the fragments and conjugate. Although CKR12 showed higher antibacterial activities than FK13 against <i>Staphylococcus aureus</i> and <i>Escherichia coli</i>, the antifungal activity of CKR12 was lower than that of FK13. CKR12-PLGA showed higher antibacterial activities against <i>S. aureus</i> and <i>E. coli</i> and higher antifungal activity against <i>Candida albicans</i> compared to those of FK13. Additionally, CKR12-PLGA showed no hemolytic activity in erythrocytes, and scanning and transmission electron microscopy suggested that CKR12-PLGA killed and disrupted the surface structure of microbial cells. Conjugation of antimicrobial peptide fragment analogues was a successful approach for obtaining increased microbial activity with minimized cytotoxicity. |
| first_indexed | 2024-03-10T11:30:22Z |
| format | Article |
| id | doaj.art-156d046f5f9947ac873f1b8f3a2e3748 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T11:30:22Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-156d046f5f9947ac873f1b8f3a2e37482023-11-21T19:17:25ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-05-012210509710.3390/ijms22105097Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against <i>Staphylococcus aureus</i>, <i>Escherichia coli</i>, and <i>Candida albicans</i>Takeshi Mori0Miyako Yoshida1Mai Hazekawa2Daisuke Ishibashi3Yoshiro Hatanaka4Toshihiro Nagao5Rie Kakehashi6Honami Kojima7Rio Uno8Minoru Ozeki9Ikuo Kawasaki10Taku Yamashita11Junichi Nishikawa12Takahiro Uchida13Faculty of Pharmaceutical Sciences, Mukogawa Women’s University, 11-68 Koshien 9-Bancho, Nishinomiya City 663-8179, JapanFaculty of Pharmaceutical Sciences, Mukogawa Women’s University, 11-68 Koshien 9-Bancho, Nishinomiya City 663-8179, JapanDepartment of Immunological and Molecular Pharmacology, Faculty of Pharmaceutical Science, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku, Fukuoka City 814-0180, JapanDepartment of Immunological and Molecular Pharmacology, Faculty of Pharmaceutical Science, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku, Fukuoka City 814-0180, JapanOsaka Research Institute of Industrial Science and Technology, 1-6-50 Morinomiya, Joto-ku, Osaka City 536-8553, JapanOsaka Research Institute of Industrial Science and Technology, 1-6-50 Morinomiya, Joto-ku, Osaka City 536-8553, JapanOsaka Research Institute of Industrial Science and Technology, 1-6-50 Morinomiya, Joto-ku, Osaka City 536-8553, JapanFaculty of Pharmaceutical Sciences, Mukogawa Women’s University, 11-68 Koshien 9-Bancho, Nishinomiya City 663-8179, JapanFaculty of Pharmaceutical Sciences, Mukogawa Women’s University, 11-68 Koshien 9-Bancho, Nishinomiya City 663-8179, JapanFaculty of Pharmaceutical Sciences, Mukogawa Women’s University, 11-68 Koshien 9-Bancho, Nishinomiya City 663-8179, JapanFaculty of Pharmaceutical Sciences, Mukogawa Women’s University, 11-68 Koshien 9-Bancho, Nishinomiya City 663-8179, JapanFaculty of Pharmaceutical Sciences, Mukogawa Women’s University, 11-68 Koshien 9-Bancho, Nishinomiya City 663-8179, JapanFaculty of Pharmaceutical Sciences, Mukogawa Women’s University, 11-68 Koshien 9-Bancho, Nishinomiya City 663-8179, JapanFaculty of Pharmaceutical Sciences, Mukogawa Women’s University, 11-68 Koshien 9-Bancho, Nishinomiya City 663-8179, JapanVarious peptides and their derivatives have been reported to exhibit antimicrobial activities. Although these activities have been examined against microorganisms, novel methods have recently emerged for conjugation of the biomaterials to improve their activities. Here, we prepared CKR12-PLGA, in which CKR12 (a mutated fragment of human cathelicidin peptide, LL-37) was conjugated with poly (lactic-co-glycolic) acid (PLGA), and compared the antimicrobial and antifungal activities of the conjugated peptide with those of FK13 (a small fragment of LL-37) and CKR12 alone. The prepared CKR12-PLGA was characterized by dynamic light scattering and measurement of the zeta potential, critical micellar concentration, and antimicrobial activities of the fragments and conjugate. Although CKR12 showed higher antibacterial activities than FK13 against <i>Staphylococcus aureus</i> and <i>Escherichia coli</i>, the antifungal activity of CKR12 was lower than that of FK13. CKR12-PLGA showed higher antibacterial activities against <i>S. aureus</i> and <i>E. coli</i> and higher antifungal activity against <i>Candida albicans</i> compared to those of FK13. Additionally, CKR12-PLGA showed no hemolytic activity in erythrocytes, and scanning and transmission electron microscopy suggested that CKR12-PLGA killed and disrupted the surface structure of microbial cells. Conjugation of antimicrobial peptide fragment analogues was a successful approach for obtaining increased microbial activity with minimized cytotoxicity.https://www.mdpi.com/1422-0067/22/10/5097antimicrobial peptidemutant peptideconjugation with poly (lactic-co-glycolic) acidscanning electron microscopytransmission electron microscopy |
| spellingShingle | Takeshi Mori Miyako Yoshida Mai Hazekawa Daisuke Ishibashi Yoshiro Hatanaka Toshihiro Nagao Rie Kakehashi Honami Kojima Rio Uno Minoru Ozeki Ikuo Kawasaki Taku Yamashita Junichi Nishikawa Takahiro Uchida Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against <i>Staphylococcus aureus</i>, <i>Escherichia coli</i>, and <i>Candida albicans</i> International Journal of Molecular Sciences antimicrobial peptide mutant peptide conjugation with poly (lactic-co-glycolic) acid scanning electron microscopy transmission electron microscopy |
| title | Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against <i>Staphylococcus aureus</i>, <i>Escherichia coli</i>, and <i>Candida albicans</i> |
| title_full | Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against <i>Staphylococcus aureus</i>, <i>Escherichia coli</i>, and <i>Candida albicans</i> |
| title_fullStr | Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against <i>Staphylococcus aureus</i>, <i>Escherichia coli</i>, and <i>Candida albicans</i> |
| title_full_unstemmed | Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against <i>Staphylococcus aureus</i>, <i>Escherichia coli</i>, and <i>Candida albicans</i> |
| title_short | Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against <i>Staphylococcus aureus</i>, <i>Escherichia coli</i>, and <i>Candida albicans</i> |
| title_sort | antimicrobial activities of ll 37 fragment mutant poly lactic co glycolic acid conjugate against i staphylococcus aureus i i escherichia coli i and i candida albicans i |
| topic | antimicrobial peptide mutant peptide conjugation with poly (lactic-co-glycolic) acid scanning electron microscopy transmission electron microscopy |
| url | https://www.mdpi.com/1422-0067/22/10/5097 |
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