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- Title
Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against Staphylococcus aureus , Escherichia coli , and Candida albicans.
- Authors
Mori, Takeshi; Yoshida, Miyako; Hazekawa, Mai; Ishibashi, Daisuke; Hatanaka, Yoshiro; Nagao, Toshihiro; Kakehashi, Rie; Kojima, Honami; Uno, Rio; Ozeki, Minoru; Kawasaki, Ikuo; Yamashita, Taku; Nishikawa, Junichi; Uchida, Takahiro; Batoni, Giovanna
- Abstract
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.
- Subjects
SCANNING transmission electron microscopy; STAPHYLOCOCCUS aureus; ESCHERICHIA coli; MICROBIAL cells; CANDIDA albicans; PEPTIDE derivatives
- Publication
International Journal of Molecular Sciences, 2021, Vol 22, Issue 10, p5097
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms22105097