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Anionic food color tartrazine enhances antibacterial efficacy of histatin-derived peptide DHVAR4 by fine-tuning its membrane activity

Published online by Cambridge University Press:  02 March 2020

Maria Ricci Open the ORCID record for Maria Ricci [Opens in a new window] ,
Kata Horváti ,
Tünde Juhász ,
Imola Szigyártó ,
György Török ,
Fanni Sebák ,
Andrea Bodor ,
László Homolya ,
Judit Henczkó  and
Bernadett Pályi
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Maria Ricci
Affiliation:
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Kata Horváti
Affiliation:
MTA-ELTE Research Group of Peptide Chemistry, Eötvös Loránd University, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Tünde Juhász
Affiliation:
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Imola Szigyártó
Affiliation:
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
György Török
Affiliation:
Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Fanni Sebák
Affiliation:
Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Budapest, H-1117, Hungary
Andrea Bodor
Affiliation:
Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Budapest, H-1117, Hungary
László Homolya
Affiliation:
Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Judit Henczkó
Affiliation:
National Public Health Center, Budapest, H-1097, Hungary
Bernadett Pályi
Affiliation:
National Public Health Center, Budapest, H-1097, Hungary
Tamás Mlinkó
Affiliation:
Laboratory of Bacteriology, Korányi National Institute for Tuberculosis and Respiratory Medicine, Budapest, H-1122, Hungary
Judith Mihály
Affiliation:
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Bilal Nizami
Affiliation:
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Zihuayuan Yang
Affiliation:
State Key Laboratory of Bioelectronics, School of Biological Science and Medical Engineering, Southeast University, Nanjing210096, China
Fengming Lin
Affiliation:
State Key Laboratory of Bioelectronics, School of Biological Science and Medical Engineering, Southeast University, Nanjing210096, China
Xiaolin Lu
Affiliation:
State Key Laboratory of Bioelectronics, School of Biological Science and Medical Engineering, Southeast University, Nanjing210096, China
Loránd Románszki
Affiliation:
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Attila Bóta
Affiliation:
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Zoltán Varga
Affiliation:
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Szilvia Bősze
Affiliation:
MTA-ELTE Research Group of Peptide Chemistry, Eötvös Loránd University, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Ferenc Zsila*
Affiliation:
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
Tamás Beke-Somfai*
Affiliation:
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary
*
Author for correspondence: Tamás Beke-Somfai, E-mail: beke-somfai.tamas@ttk.mta.hu; Ferenc Zsila, E-mail: zsila.ferenc@ttk.mta.hu
Author for correspondence: Tamás Beke-Somfai, E-mail: beke-somfai.tamas@ttk.mta.hu; Ferenc Zsila, E-mail: zsila.ferenc@ttk.mta.hu
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Abstract

Here it is demonstrated how some anionic food additives commonly used in our diet, such as tartrazine (TZ), bind to DHVAR4, an antimicrobial peptide (AMP) derived from oral host defense peptides, resulting in significantly fostered toxic activity against both Gram-positive and Gram-negative bacteria, but not against mammalian cells. Biophysical studies on the DHVAR4–TZ interaction indicate that initially large, positively charged aggregates are formed, but in the presence of lipid bilayers, they rather associate with the membrane surface. In contrast to synergistic effects observed for mixed antibacterial compounds, this is a principally different mechanism, where TZ directly acts on the membrane-associated AMP promoting its biologically active helical conformation. Model vesicle studies show that compared to dye-free DHVAR4, peptide–TZ complexes are more prone to form H-bonds with the phosphate ester moiety of the bilayer head-group region resulting in more controlled bilayer fusion mechanism and concerted severe cell damage. AMPs are considered as promising compounds to combat formidable antibiotic-resistant bacterial infections; however, we know very little on their in vivo actions, especially on how they interact with other chemical agents. The current example illustrates how food dyes can modulate AMP activity, which is hoped to inspire improved therapies against microbial infections in the alimentary tract. Results also imply that the structure and function of natural AMPs could be manipulated by small compounds, which may also offer a new strategic concept for the future design of peptide-based antimicrobials.

Keywords

Aggregationantimicrobial peptidesfood colorsmembrane biophysicsmolecular mechanism
Type
Report
Information
Quarterly Reviews of Biophysics , Volume 53 , 2020 , e5
Copyright
Copyright © The Author(s), 2020. Published by Cambridge University Press

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