Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide |
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| Authors: | Shuli Chou Qiuke Li Hua Wu Jinze Li Yung-Fu Chang Lu Shang Jiawei Li Zhihua Wang Anshan Shan |
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| Affiliation: | 1.Institute of Animal Nutrition, Northeast Agricultural University, Harbin 150030, China; (S.C.); (Q.L.); (H.W.); (J.L.); (L.S.); (J.L.); (Z.W.);2.Department of Population Medicine and Diagnostic Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA; |
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| Abstract: | Candida albicans, an opportunistic fungus, causes dental caries and contributes to mucosal bacterial dysbiosis leading to a second infection. Furthermore, C.albicans forms biofilms that are resistant to medicinal treatment. To make matters worse, antifungal resistance has spread (albeit slowly) in this species. Thus, it has been imperative to develop novel, antifungal drug compounds. Herein, a peptide was engineered with the sequence of RRFSFWFSFRR-NH2; this was named P19. This novel peptide has been observed to exert disruptive effects on fungal cell membrane physiology. Our results showed that P19 displayed high binding affinity to lipopolysaccharides (LPS), lipoteichoic acids (LTA) and the plasma membrane phosphatidylinositol (PI), phosphatidylserine (PS), cardiolipin, and phosphatidylglycerol (PG), further indicating that the molecular mechanism of P19 was not associated with the receptor recognition, but rather related to competitive interaction with the plasma membrane. In addition, compared with fluconazole and amphotericin B, P19 has been shown to have a lower potential for resistance selection than established antifungal agents. |
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| Keywords: | Tryptophan center symmetrical short peptide fungus-targeted activity and biofilm inhibition low drug resistance and side-effects |
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