The antimicrobial peptide CGA-N12 (NH2-ALQGAKERAHQQ-COOH) is an active peptide derived from chromogranin A (CGA) and consists of the 65th to 76th amino acids of the N-terminus. The results of our previous studies showed that CGA-N12 exerts anti-Candida activity by inducing apoptosis without destroying the integrity of cell membranes. In this study, the effect of CGA-N12 on the cell membrane structure of Candida tropicalis was investigated. CGA-N12 resulted in the dissipation of the membrane potential, the increase in membrane fluidity, and the outflow of potassium ions in C. tropicalis without significantly changing the ergosterol level. Fluorescence quenching was applied to evaluate the membrane channel characteristics induced by CGA-N12 through detection of the following: membrane permeability of hydrated Cl− (ϕ ≈ 0.66 nm) using the membrane-impermeable halogen anion-selective fluorescent dye lucigenin, passage of the membrane-impermeable dye carboxyfluorescein (CF) (ϕ ≈ 1 nm) through the membrane, and membrane permeation of H3O+ based on the membrane non-permeable pH-sensitive fluorescent dye 8-hydroxypyrene-1,3,6-trisulfonic acid, trisodium salt (HPTS). In conclusion, CGA-N12 can induce the formation of non-selective ion channels <1 nm in diameter in the membranes of C. tropicalis, resulting in the leakage of potassium ions, chloride ions, and protons, among others, leading to dissipation of the membrane potential. As a result, the fluidity of membranes is increased without destroying the synthesis of ergosterol is not affected.
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May 2020
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Cover Image
The cover image shows high resolution of the 20 lowest energy structures of kringle 2 of human plasminogen to AGL55-NS88.2 (top) and KT155-SS1448 (bottom). To learn more about this, see the article by Qiu and colleagues (pp. 1613–1630). The image was provided by Francis J. Castellino.
Research Article|
May 21 2020
Effects of CGA-N12 on the membrane structure of Candida tropicalis cells
Ruifang Li
;
1College of Bioengineering, Henan University of Technology, Zhengzhou, Henan 450001, P. R. China
Correspondence: Ruifang Li (lrf@haut.edu.cn)
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Weini Shi;
Weini Shi
1College of Bioengineering, Henan University of Technology, Zhengzhou, Henan 450001, P. R. China
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Ruiling Zhang;
Ruiling Zhang
2College of Chemistry, Beijing Normal University, Beijing 100875, P. R. China
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Liang Huang;
Liang Huang
1College of Bioengineering, Henan University of Technology, Zhengzhou, Henan 450001, P. R. China
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Yanjie Yi;
Yanjie Yi
1College of Bioengineering, Henan University of Technology, Zhengzhou, Henan 450001, P. R. China
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Aihua Li;
Aihua Li
3School of Distance and Continuing Education, Henan University of Technology, Zhengzhou, Henan 450001, P. R. China
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Hongjuan Jing;
Hongjuan Jing
1College of Bioengineering, Henan University of Technology, Zhengzhou, Henan 450001, P. R. China
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Mengke Tao;
Mengke Tao
1College of Bioengineering, Henan University of Technology, Zhengzhou, Henan 450001, P. R. China
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Meng Zhang;
Meng Zhang
1College of Bioengineering, Henan University of Technology, Zhengzhou, Henan 450001, P. R. China
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Nanqi Pei
Nanqi Pei
1College of Bioengineering, Henan University of Technology, Zhengzhou, Henan 450001, P. R. China
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Publisher: Portland Press Ltd
Received:
December 19 2019
Revision Received:
April 24 2020
Accepted:
April 29 2020
Accepted Manuscript online:
April 29 2020
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2020
Biochem J (2020) 477 (10): 1813–1825.
Article history
Received:
December 19 2019
Revision Received:
April 24 2020
Accepted:
April 29 2020
Accepted Manuscript online:
April 29 2020
Citation
Ruifang Li, Weini Shi, Ruiling Zhang, Liang Huang, Yanjie Yi, Aihua Li, Hongjuan Jing, Mengke Tao, Meng Zhang, Nanqi Pei; Effects of CGA-N12 on the membrane structure of Candida tropicalis cells. Biochem J 29 May 2020; 477 (10): 1813–1825. doi: https://doi.org/10.1042/BCJ20190939
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