Alkylamidobetaines Induced Changes in Multidrug-Resistant, Biofilming Candidaglabrata—Analysis of Oxidative Stress and Cellular Proteome
8 affiliations
- 1Department of Biochemistry and Immunochemistry, Wroclaw Medical University, Ul. Chałubińskiego 10, 50-368 Wroclaw, Poland
- 2Department of Microbiology, Faculty of Medicine, Wroclaw Medical University, Ul. Chałubińskiego 4, 50-376 Wroclaw, Poland
- 3Faculty of Medicine, SKN Medical Image Analysis and Research in Pathology (MIARP), Wroclaw Medical University, Wyb. Pasteura 1, 50-375 Wroclaw, Poland
- 4Department of Pharmacognosy and Herbal Medicines, Wroclaw Medical University, Ul. Borowska 211a, 50-556 Wrocław, Poland
- 5Department of Pharmaceutical Microbiology and Parasitology, Wroclaw Medical University, Ul. Borowska 211a, 50-556 Wrocław, Poland
- 6Core Facility for Mass Spectrometry and Proteomics, Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 329, 69120 Heidelberg, Germany
- 7Department of Pharmacognosy with Medicinal Plants Garden, Lublin Medical University, Ul. Chodźki 1, 20-093 Lublin, Poland
- 8Department of Engineering and Technology of Chemical Processes, Wroclaw University of Science and Technology, Norwida 4/6, 50-373 Wroclaw, Poland
Abstract
Antibiofilm strategies targeting Candida glabrata increasingly focus on membrane-active compounds capable of disrupting biofilm formation and mature biofilm structure. Building on previous work identifying alkylamidobetaine C9 (AAB C9)—[(3-decanoylmethylamino)propyl]dimethylammonium acetate—and β-escin as antibiofilm agents against C. glabrata, this study examined the biochemical and physiological basis of their efficacy in a reference strain (ATCC 90030) and a clinical isolate (2586). Oxidative stress was assessed microscopically after two hours of exposure, and proteome changes were quantified after six hours, for each compound alone and in combination. Fluorescence microscopy showed that AAB C9 and β-escin interacted differently depending on the ROS compartment and strain: in the strain ATCC 90030, the combination antagonized β-escin-induced mitochondrial superoxide, whereas in the multidrug-resistant isolate 2586 it exceeded either agent alone for both cytosolic and mitochondrial superoxide, indicating a strain-dependent, additive interaction. Quantitative proteomics showed that strain genetic background, rather than treatment, was the dominant source of proteome variance. Preranked gene set enrichment analysis revealed that AAB C9 significantly suppressed accumulation of biofilm-formation-associated proteins specifically in isolate 2586, corroborating its phenotypic antibiofilm activity, while β-escin and the combination produced opposing transmembrane-transport signatures, pointing to compound-specific mechanisms underlying their differential antifungal and antibiofilm effects.
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BibTeX
@article{bromke2026alkylamidobetaines,
title = {{Alkylamidobetaines Induced Changes in Multidrug-Resistant, Biofilming Candidaglabrata—Analysis of Oxidative Stress and Cellular Proteome}},
author = {Mariusz A. Bromke and Emilia Nowak and Olga Bortkiewicz and Bartosz Poniewierka and Michał Gleńsk and Urszula Nawrot and Marcin Luzarowski and Jarosław Widelski and Łukasz Lamch and Kazimiera A. Wilk and Emil Paluch},
journal = {International Journal of Molecular Sciences},
year = {2026},
month = sep,
doi = {10.3390/ijms27188309},
url = {https://www.mdpi.com/1422-0067/27/18/8309},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Alkylamidobetaines Induced Changes in Multidrug-Resistant, Biofilming Candidaglabrata—Analysis of Oxidative Stress and Cellular Proteome
AU - Mariusz A. Bromke
AU - Emilia Nowak
AU - Olga Bortkiewicz
AU - Bartosz Poniewierka
AU - Michał Gleńsk
AU - Urszula Nawrot
AU - Marcin Luzarowski
AU - Jarosław Widelski
AU - Łukasz Lamch
AU - Kazimiera A. Wilk
AU - Emil Paluch
PY - 2026
DA - 2026/09/18
JO - International Journal of Molecular Sciences
DO - 10.3390/ijms27188309
UR - https://www.mdpi.com/1422-0067/27/18/8309
AB - Antibiofilm strategies targeting Candida glabrata increasingly focus on membrane-active compounds capable of disrupting biofilm formation and mature biofilm structure. Building on previous work identifying alkylamidobetaine C9 (AAB C9)—[(3-decanoylmethylamino)propyl]dimethylammonium acetate—and β-escin as antibiofilm agents against C. glabrata, this study examined the biochemical and physiological basis of their efficacy in a reference strain (ATCC 90030) and a clinical isolate (2586). Oxidative stress was assessed microscopically after two hours of exposure, and proteome changes were quantified after six hours, for each compound alone and in combination. Fluorescence microscopy showed that AAB C9 and β-escin interacted differently depending on the ROS compartment and strain: in the strain ATCC 90030, the combination antagonized β-escin-induced mitochondrial superoxide, whereas in the multidrug-resistant isolate 2586 it exceeded either agent alone for both cytosolic and mitochondrial superoxide, indicating a strain-dependent, additive interaction. Quantitative proteomics showed that strain genetic background, rather than treatment, was the dominant source of proteome variance. Preranked gene set enrichment analysis revealed that AAB C9 significantly suppressed accumulation of biofilm-formation-associated proteins specifically in isolate 2586, corroborating its phenotypic antibiofilm activity, while β-escin and the combination produced opposing transmembrane-transport signatures, pointing to compound-specific mechanisms underlying their differential antifungal and antibiofilm effects.
SN - 1422-0067
ER -