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Article

Hydrophilic Linear Peptide with Histidine and Lysine Residues as a Key Factor Affecting Antifungal Activity

1
Department of Polymer Science and Engineering, Sunchon National University, Suncheon, Jeonnam 57922, Korea
2
Division of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Gyeongnam 52828, Korea
3
Department of Nutrition and Food Science, Texas A&M University, College Station, TX 77843, USA
4
National Institute of Ecology (NIE), Seocheon, Choongnam 33657, Korea
5
The Research Institute for Sanitation and Environment of Coastal Areas, Sunchon National University, Suncheon, Jeonnam 57922, Korea
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2018, 19(12), 3781; https://doi.org/10.3390/ijms19123781
Received: 30 October 2018 / Revised: 23 November 2018 / Accepted: 24 November 2018 / Published: 28 November 2018
(This article belongs to the Section Molecular Microbiology)
Increases in the numbers of immunocompromised patients and the emergence of drug-resistance fungal pathogens have led to the need for new, safe, efficacious antifungal agents. In this study, we designed a histidine-lysine-lysine (HKK) motif and synthesized six HKK peptides with repetitions of the motif. These peptides showed length-dependent antifungal activity against drug-susceptible and drug-resistant fungal pathogens via membranolytic or non-membranolytic action. None of the peptides were cytotoxic to rat erythrocytes or NIH3T3 mouse embryonic fibroblasts. Short-length peptides were directly translocated in fungal cytosol and reacted with mitochondria, resulting in apoptosis. Membrane-permeabilizing activity occurred in the presence of long peptides, and peptides were able to transfer to the cytosol and induce reactive oxygen species. Our results suggest that peptides composed only of cationic amino acids may be good candidates as antifungal agents. View Full-Text
Keywords: antimicrobial peptide; drug-resistance; antifungal activity; reactive oxygen species; apoptosis antimicrobial peptide; drug-resistance; antifungal activity; reactive oxygen species; apoptosis
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MDPI and ACS Style

Park, S.-C.; Kim, J.-Y.; Kim, E.-J.; Cheong, G.-W.; Lee, Y.; Choi, W.; Lee, J.R.; Jang, M.-K. Hydrophilic Linear Peptide with Histidine and Lysine Residues as a Key Factor Affecting Antifungal Activity. Int. J. Mol. Sci. 2018, 19, 3781. https://doi.org/10.3390/ijms19123781

AMA Style

Park S-C, Kim J-Y, Kim E-J, Cheong G-W, Lee Y, Choi W, Lee JR, Jang M-K. Hydrophilic Linear Peptide with Histidine and Lysine Residues as a Key Factor Affecting Antifungal Activity. International Journal of Molecular Sciences. 2018; 19(12):3781. https://doi.org/10.3390/ijms19123781

Chicago/Turabian Style

Park, Seong-Cheol, Jin-Young Kim, Eun-Ji Kim, Gang-Won Cheong, Yongjae Lee, Wonkyun Choi, Jung R. Lee, and Mi-Kyeong Jang. 2018. "Hydrophilic Linear Peptide with Histidine and Lysine Residues as a Key Factor Affecting Antifungal Activity" International Journal of Molecular Sciences 19, no. 12: 3781. https://doi.org/10.3390/ijms19123781

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