1. Jacalin-copper sulfide nanoparticles complex enhance the antibacterial activity against drug resistant bacteria via cell surface glycan recognition.
- Author
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Ahmed KBA, Subramaniyan SB, Banu SF, Nithyanand P, and Veerappan A
- Subjects
- Aeromonas drug effects, Animals, Cell Membrane drug effects, Escherichia coli drug effects, Humans, Kinetics, Materials Testing, Microbial Sensitivity Tests, Reactive Oxygen Species metabolism, Spectrometry, Fluorescence, Zebrafish, Anti-Bacterial Agents pharmacology, Cell Membrane metabolism, Copper pharmacology, Drug Resistance, Bacterial drug effects, Nanoparticles chemistry, Plant Lectins pharmacology, Polysaccharides metabolism, Sulfides pharmacology
- Abstract
In any therapeutic modality the usage of drug in high doses often leads to serious side-effects. Herein, we demonstrated a method to enhance the antibacterial efficacy of CuS NPs at lower concentration through interacting with jackfruit seed lectin, jacalin. Fluorescence quenching studies revealed that jacalin form complex with CuS NPs and the association constant was 1.91 × 10
4 M-1 . Upon complex with jacalin, the bacterial minimum inhibitory concentration (MIC) of CuS NPs drastically decreases from 12.5 μM to 0.78 μM. The addition of jacalin specific sugar, galactose to jacalin-CuS NPs complex (JCuS NPs) reverses the MIC from 0.78 μM to 25 μM. Mechanistic study suggests that JCuS NPs kills bacteria in part by reactive oxygen species and membrane damage, but galactose prevents the action of JCuS NPs at 0.78 μM. JCuS NPs successfully reduce (14 fold) A. hydrophila colonization in an infected zerbra fish and rescue them completely from the infection, but galJCuS NPs and CuS NPs were ineffective at 0.78 μM. Collectively, our studies demonstrates that the enhance antibacterial activity of JCuS NPs is likely due to the interaction between the galactose binding site of jacalin and the bacterial strains, as a result NPs are targeted and delivered sufficiently., (Copyright © 2017 Elsevier B.V. All rights reserved.)- Published
- 2018
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