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Volume 22
Issue 15
10.3390/ijms22158231
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Article

Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide

by
Shuli Chou
1,
Qiuke Li
1,
Hua Wu
1,
Jinze Li
1,
Yung-Fu Chang
2,
Lu Shang
1,
Jiawei Li
1,
Zhihua Wang
1 and
Anshan Shan
1,*
1
Institute of Animal Nutrition, Northeast Agricultural University, Harbin 150030, China
2
Department of Population Medicine and Diagnostic Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2021, 22(15), 8231; https://doi.org/10.3390/ijms22158231
Submission received: 1 July 2021 / Revised: 19 July 2021 / Accepted: 19 July 2021 / Published: 30 July 2021
(This article belongs to the Special Issue Recent Advances on Small Molecule for Multitarget-Based Treatment of Human Diseases)
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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.
Keywords: Tryptophan center symmetrical short peptide; fungus-targeted activity and biofilm inhibition; low drug resistance and side-effects Tryptophan center symmetrical short peptide; fungus-targeted activity and biofilm inhibition; low drug resistance and side-effects

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MDPI and ACS Style

Chou, S.; Li, Q.; Wu, H.; Li, J.; Chang, Y.-F.; Shang, L.; Li, J.; Wang, Z.; Shan, A. Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide. Int. J. Mol. Sci. 2021, 22, 8231. https://doi.org/10.3390/ijms22158231

AMA Style

Chou S, Li Q, Wu H, Li J, Chang Y-F, Shang L, Li J, Wang Z, Shan A. Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide. International Journal of Molecular Sciences. 2021; 22(15):8231. https://doi.org/10.3390/ijms22158231

Chicago/Turabian Style

Chou, Shuli, Qiuke Li, Hua Wu, Jinze Li, Yung-Fu Chang, Lu Shang, Jiawei Li, Zhihua Wang, and Anshan Shan. 2021. "Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide" International Journal of Molecular Sciences 22, no. 15: 8231. https://doi.org/10.3390/ijms22158231

APA Style

Chou, S., Li, Q., Wu, H., Li, J., Chang, Y.-F., Shang, L., Li, J., Wang, Z., & Shan, A. (2021). Selective Antifungal Activity and Fungal Biofilm Inhibition of Tryptophan Center Symmetrical Short Peptide. International Journal of Molecular Sciences, 22(15), 8231. https://doi.org/10.3390/ijms22158231

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