Spectroscopic investigation on the interaction of ruthenium complexes with tumor specific lectin, jacalin

Ahmed, Khawaja Ashfaque; Reshma, Elamvazhuthi; Mariappan, Mariappan; Veerappan, Anbazhagan

doi:10.1016/j.saa.2014.09.047

Cited by 14 publications

(9 citation statements)

References 66 publications

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“…These results suggest that the quenching process is static and a nonfluorescent complex is likely formed between BSA and pCuS. From the quenching study, the binding constant ( K a ) was calculated by the following expression. , where F ∞ is the change in fluorescence intensity at infinite pCuS concentration, n is the number of binding sites, and K a is the association constant. F ∞ was obtained from the ordinate intercept of the plot of F 0 /Δ F ∞ versus 1/[pCuS].…”

Section: Resultsmentioning

confidence: 99%

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Remarkable Effect of Jacalin in Diminishing the Protein Corona Interference in the Antibacterial Activity of Pectin-Capped Copper Sulfide Nanoparticles

et al. 2019

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Herein, we report a new strategy based on jacalin functionalization to diminish the impact of biological fluids in the antibacterial applications of nanoparticles (NPs). Precoating pectin-capped copper sulfide NPs (pCuS) with bovine serum albumin produced a protein corona, which affects the antibacterial activity of pCuS. It was found that the minimum inhibitory concentration (MIC) increases fourfold because of the formation of the protein corona. Interestingly, the pCuS functionalized with jacalin enhance the targeting capabilities through bacterial cell surface glycan recognition with no interference from the protein corona. The MIC of pCuS decreases 16-fold on functionalization with jacalin. Mechanistic studies indicated that the pCuS functionalized with jacalin impede the protein corona interference and induce bacterial cell death by impairing the GSH/reactive oxygen species balance and disrupting the bacteria cell membrane. As a proof of concept, we used a bacteria-infected zebrafish animal model to demonstrate the interference of biological fluids in the antibacterial activity of NPs. Infected zebrafish treated with 1× MIC of pCuS failed to recover from the infection, but 4× MIC rescues the fish. The requirement of a high dose of NPs to treat the infection confirms the interference of biological fluids in nanotherapeutic applications. At the same time, the jacalin–pCuS complex rescues the infected fish at 16-fold lesser MIC. The results obtained from this study suggest that jacalin-mediated NP targeting may have broad implications in the development of future nanomedicine.

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Section: Resultsmentioning

confidence: 99%

“…From the quenching study, the binding constant (K a ) was calculated by the following expression. 28,29…”

Section: F Fmentioning

confidence: 99%

Remarkable Effect of Jacalin in Diminishing the Protein Corona Interference in the Antibacterial Activity of Pectin-Capped Copper Sulfide Nanoparticles

et al. 2019

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“…The cell wall of UPEC is rich in negative charge and lipopolysaccharide. − The saccharide binding site of BMSL was reported to recognize the bacterial cell surface glycans; thus, a noncovalent complex of cNAEs and BMSL was prepared by incubating the cNAEs–BMSL mixture at 4 °C for 2 h. The strength of complex formation was investigated by binding studies using fluorescence spectroscopy and molecular docking. Lectin fluorophores are highly sensitive to the binding of specific and nonspecific ligands. − The fluorescence emission of BMSL originates from tryptophan, and tyrosine residues in the presence of an increasing concentration of cN16E are shown in Figure S5 (see the Supporting Information). It is noted from Figure S5, the intensity at emission maxima 337 nm was quenched upon titrating with cN16E, indicating the binding between cN16E and BMSL.…”

Section: Resultsmentioning

confidence: 96%

Dual Function Antimicrobial Loaded Lectin Carrier: A Strategy to Overcome Biomolecular Interference without Detectable Resistance

et al. 2021

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The disposition of a drug in a biological system may be altered by complex biological fluids; especially, protein binding to drugs influences their activity. Herein, we demonstrated a convenient method involving the noncovalent formulation of butea monosperma seed lectin (BMSL) with an antimicrobial lipid, cationic N-acylethanolamine (cNAE) to mitigate the serum protein interference. Fluorescence spectroscopy and molecular docking study revealed that cNAEs readily formed noncovalent complexes with serum protein, bovine serum albumin. The resulting complexes interfered with the antimicrobial activity of cNAEs. Strikingly, the noncovalent conjugates developed with BMSL and cNAEs (BcNAE) overcame the interference from serum protein and displayed remarkable antimicrobial activity against uropathogenic Escherichia coli (UPEC). Strikingly, the minimum inhibitory concentration (MIC) of the lectin conjugates (7.81 μM) was 4-fold lower than the MIC of pure cNAE. Mechanistic studies showed that BcNAE depolarized the bacterial membrane and affected the integrity to exert the antimicrobial activity. The membrane directed activities of BcNAE on UPEC efficiently eliminated the development of resistance even after 25 passages. The hemocompatibility results and the biosafety assessed in a zebrafish model suggested that BcNAE was nontoxic with good selectivity to bacteria. While testing the therapeutic efficacy against UPEC infected zebrafish, we found that 1× MIC cNAE is ineffective due to interference from biological fluids, which is in agreement with in vitro studies. Remarkably, the infected fish treated with 1× MIC BcNAE conjugates were rescued from infection and restored to the normal life in less than 9 h. Bacterial colony count assay revealed that BcNAE was more efficient in overcoming the biological fluid interference and eliminated the bacterial burden in infected zebrafish. Histopathology analysis supported that BcNAE treatment restored the pathological changes induced by UPEC and, thus, increased survival. The high antimicrobial intensity with limited chance for resistance development and potential to overcome biomolecular interference with a lack of toxicity enhance the merits of exploring lectin conjugates against infectious pathogens.

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“…That interest in the bioactivity profiles of ruthenium complexes has grown rapidly is amply demonstrated by design of new Ru compounds inhibiting enzymes, by the novel multinuclear systems acting as drug delivery vehicles or imaging and theranostics agents and signal transduction elements. A major contribution came as well from the advent of refined bioanalytical, biophysical and spectroscopic techniques used to elucidate the structure and the in vivo functioning of these complexes [79,80,81,82,83,84,85,86,87,88,89,90,91,92,93,94,95,96,97,98,99,100]. Some arene-functionalized dinuclear organometallic Ru(II) complexes are capable of crosslinking model peptide and oligonucleotide sequences while cytotoxicities are linked to their more rigid or more flexible conformations [81].…”

Section: Ruthenium-based Anticancer Drugs Medicinal Applicationsmentioning

confidence: 99%

Editorial of Special Issue Ruthenium Complex: The Expanding Chemistry of the Ruthenium Complexes

Drăguţan

Demonceau

2015

Molecules

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Spectroscopic investigation on the interaction of ruthenium complexes with tumor specific lectin, jacalin

Cited by 14 publications

References 66 publications

Remarkable Effect of Jacalin in Diminishing the Protein Corona Interference in the Antibacterial Activity of Pectin-Capped Copper Sulfide Nanoparticles

Remarkable Effect of Jacalin in Diminishing the Protein Corona Interference in the Antibacterial Activity of Pectin-Capped Copper Sulfide Nanoparticles

Dual Function Antimicrobial Loaded Lectin Carrier: A Strategy to Overcome Biomolecular Interference without Detectable Resistance

Editorial of Special Issue Ruthenium Complex: The Expanding Chemistry of the Ruthenium Complexes

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