Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against Staphylococcus aureus, Escherichia coli, and Candida albicans
| Autor: | Rie Kakehashi, Takeshi Mori, Daisuke Ishibashi, Honami Kojima, Takahiro Uchida, Toshihiro Nagao, Ikuo Kawasaki, Taku Yamashita, Minoru Ozeki, Miyako Yoshida, Rio Uno, Mai Hazekawa, Jun-ichi Nishikawa, Yoshiro Hatanaka |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
antimicrobial peptide QH301-705.5 medicine.medical_treatment Peptide macromolecular substances medicine.disease_cause Catalysis Cathelicidin Microbiology Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine transmission electron microscopy medicine Physical and Theoretical Chemistry Biology (General) Candida albicans Molecular Biology Escherichia coli QD1-999 Spectroscopy chemistry.chemical_classification mutant peptide biology Chemistry conjugation with poly (lactic-co-glycolic) acid Organic Chemistry technology industry and agriculture General Medicine Antimicrobial biology.organism_classification Computer Science Applications PLGA 030104 developmental biology Staphylococcus aureus 030220 oncology & carcinogenesis scanning electron microscopy Conjugate |
| Zdroj: | International Journal of Molecular Sciences Volume 22 Issue 10 International Journal of Molecular Sciences, Vol 22, Iss 5097, p 5097 (2021) |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms22105097 |
| Popis: | 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 Staphylococcus aureus and Escherichia coli, the antifungal activity of CKR12 was lower than that of FK13. CKR12-PLGA showed higher antibacterial activities against S. aureus and E. coli and higher antifungal activity against Candida albicans 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. |
| Databáze: | OpenAIRE |
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