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Volume 21
Issue 7
10.3390/ijms21072654
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Article

The Interactions between the Antimicrobial Peptide P-113 and Living Candida albicans Cells Shed Light on Mechanisms of Antifungal Activity and Resistance

by
Kuang-Ting Cheng
1,†,
Chih-Lung Wu
1,†,
Bak-Sau Yip
1,2,†,
Ya-Han Chih
1,
Kuang-Li Peng
1,
Su-Ya Hsu
1,
Hui-Yuan Yu
1 and
Jya-Wei Cheng
1,*
1
Institute of Biotechnology and Department of Medical Science, National Tsing Hua University, Hsinchu 300, Taiwan
2
Department of Neurology, National Taiwan University Hospital Hsinchu Branch, Hsinchu 300, Taiwan
*
Author to whom correspondence should be addressed.
†
These authors contributed equally to this work.
Int. J. Mol. Sci. 2020, 21(7), 2654; https://doi.org/10.3390/ijms21072654
Received: 22 March 2020 / Revised: 7 April 2020 / Accepted: 8 April 2020 / Published: 10 April 2020
(This article belongs to the Special Issue Selected Papers from the 8th Asia-Pacific NMR Symposium (APNMR): Recent Advances in NMR Spectroscopy)
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Abstract

In the absence of proper immunity, such as in the case of acquired immune deficiency syndrome (AIDS) patients, Candida albicans, the most common human fungal pathogen, may cause mucosal and even life-threatening systemic infections. P-113 (AKRHHGYKRKFH), an antimicrobial peptide (AMP) derived from the human salivary protein histatin 5, shows good safety and efficacy profiles in gingivitis and human immunodeficiency virus (HIV) patients with oral candidiasis. However, little is known about how P-113 interacts with Candida albicans or its degradation by Candida-secreted proteases that contribute to the fungi’s resistance. Here, we use solution nuclear magnetic resonance (NMR) methods to elucidate the molecular mechanism of interactions between P-113 and living Candida albicans cells. Furthermore, we found that proteolytic cleavage of the C-terminus prevents the entry of P-113 into cells and that increasing the hydrophobicity of the peptide can significantly increase its antifungal activity. These results could help in the design of novel antimicrobial peptides that have enhanced stability in vivo and that can have potential therapeutic applications. View Full-Text
Keywords: antimicrobial peptide; Candida albicans; protease; non-natural amino acid; NMR antimicrobial peptide; Candida albicans; protease; non-natural amino acid; NMR
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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MDPI and ACS Style

Cheng, K.-T.; Wu, C.-L.; Yip, B.-S.; Chih, Y.-H.; Peng, K.-L.; Hsu, S.-Y.; Yu, H.-Y.; Cheng, J.-W. The Interactions between the Antimicrobial Peptide P-113 and Living Candida albicans Cells Shed Light on Mechanisms of Antifungal Activity and Resistance. Int. J. Mol. Sci. 2020, 21, 2654. https://doi.org/10.3390/ijms21072654

AMA Style

Cheng K-T, Wu C-L, Yip B-S, Chih Y-H, Peng K-L, Hsu S-Y, Yu H-Y, Cheng J-W. The Interactions between the Antimicrobial Peptide P-113 and Living Candida albicans Cells Shed Light on Mechanisms of Antifungal Activity and Resistance. International Journal of Molecular Sciences. 2020; 21(7):2654. https://doi.org/10.3390/ijms21072654

Chicago/Turabian Style

Cheng, Kuang-Ting, Chih-Lung Wu, Bak-Sau Yip, Ya-Han Chih, Kuang-Li Peng, Su-Ya Hsu, Hui-Yuan Yu, and Jya-Wei Cheng. 2020. "The Interactions between the Antimicrobial Peptide P-113 and Living Candida albicans Cells Shed Light on Mechanisms of Antifungal Activity and Resistance" International Journal of Molecular Sciences 21, no. 7: 2654. https://doi.org/10.3390/ijms21072654

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