Investigation of effects of newly synthesized Pt(II) complex against human serum albumin and leukemia cell line of K562

The aim of this study was to determine the cytotoxic effect of 3-arylidenechromanone (1) and 3arylideneflavanone (2) on HL-60 and NALM-6 cell lines (two human leukemia cell lines) and a WM-115 melanoma cell line. Both compounds exhibited high cytotoxic activity with higher cytotoxicity exerted by compound 2, for which IC50 values below 10 µM were found for each cell line. For compound 1, the IC50 values were higher than 10 µM for HL-60 and WM-115 cell lines, but IC50 < 10 µM was found for the NALM-6 cell line. Both compounds, at the concentrations close to IC50 (concentration range: 5–24 µM/L for compound 1 and 6–10 µM/L for compound 2), are not toxic towards red blood cells. The synthesized compounds were characterized using spectroscopic methods 1H- and 13C-NMR, IR, MS, elemental analysis, and X-ray diffraction. The lipophilicity of both synthesized compounds was determined using an RP-TLC method and the logP values found were compared with the theoretical ones taken from the Molinspiration Cheminformatics (miLogP) software package. The mode of binding of both compounds to human serum albumin was assessed using molecular docking methods.

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Pyrazolo[3,4-d]pyrimidines-loaded human serum albumin (HSA) nanoparticles: Preparation, characterization and cytotoxicity evaluation against neuroblastoma cell line

Bioorganic & Medicinal Chemistry Letters ◽

10.1016/j.bmcl.2017.05.015 ◽

2017 ◽

Vol 27 (14) ◽

pp. 3196-3200 ◽

Cited By ~ 8

Author(s):

Anna Lucia Fallacara ◽

Arianna Mancini ◽

Claudio Zamperini ◽

Elena Dreassi ◽

Stefano Marianelli ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Cell Line ◽

Neuroblastoma Cell ◽

Neuroblastoma Cell Line

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Adherence of Streptococcus pneumoniae to Respiratory Epithelial Cells Is Inhibited by Sialylated Oligosaccharides

Infection and Immunity ◽

10.1128/iai.66.4.1439-1444.1998 ◽

1998 ◽

Vol 66 (4) ◽

pp. 1439-1444 ◽

Cited By ~ 69

Author(s):

Roger Barthelson ◽

Ali Mobasseri ◽

David Zopf ◽

Paul Simon

Keyword(s):

Streptococcus Pneumoniae ◽

Human Serum Albumin ◽

Epithelial Cells ◽

Serum Albumin ◽

Human Serum ◽

Cell Line ◽

Airway Epithelial Cells ◽

Logarithmic Phase ◽

Respiratory Epithelial Cells ◽

Respiratory Epithelial

ABSTRACT To study carbohydrate-mediated adherence of Streptococcus pneumoniae to the human airway, we measured binding of liveS. pneumoniae organisms to a cultured cell line derived from the lining of the conjunctiva and to primary monolayers of human bronchial epithelial cells in the presence and absence of oligosaccharide inhibitors. Both encapsulated and nonencapsulated strains of S. pneumoniae grown to mid-logarithmic phase in suspension culture adhered to cultured primary respiratory epithelial cells and the conjunctival cell line. Adherence of nine clinically prevalent S. pneumoniaecapsular types studied was inhibited preferentially by sialylated oligosaccharides that terminate with the disaccharide NeuAcα2-3(or 6)Galβ1. Adherence of some strains also was weakly inhibited by oligosaccharides that terminate with lactosamine (Galβ1-4GlcNAcβ1). When sialylated oligosaccharides were covalently coupled to human serum albumin at a density of approximately 20 oligosaccharides per molecule of protein, the molar inhibitory potency of the oligosaccharide inhibitor was enhanced 500-fold. The above-mentioned experiments reveal a previously unreported dependence upon sialylated carbohydrate ligands for adherence of S. pneumoniae to human upper airway epithelial cells. Enhanced inhibitory potencies of polyvalent over monovalent forms of oligosaccharide inhibitors of adherence suggest that the putative adhesin(s) that recognizes the structure NeuAcα2-3(or 6)Galβ1 is arranged on the bacterial surface in such a manner that it may be cross-linked by oligosaccharides covalently linked to human serum albumin.

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Designing of a Novel Scaffold Based on Human Serum Albumin and Hydroxyapatite Nanoparticles, and the Study of Its Cytotoxic Effects on the Spermatogonia Cell Line

Journal of Biomaterials and Tissue Engineering ◽

10.1166/jbt.2014.1209 ◽

2014 ◽

Vol 4 (8) ◽

pp. 638-644 ◽

Cited By ~ 2

Author(s):

Ali Jebali ◽

Seyedhossein Hekmatimoghaddam ◽

Saeide Nezami Ganjavi ◽

Mona Yadegar

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Cell Line ◽

Hydroxyapatite Nanoparticles ◽

Cytotoxic Effects ◽

Spermatogonia Cell ◽

Novel Scaffold

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Coomassie Bright Blue-Conjugated Human Serum Albumin Nanoparticles as a Tumor-Selective Weapon for Leukemia Therapy

Nanoscience and Nanotechnology Letters ◽

10.1166/nnl.2019.3067 ◽

2019 ◽

Vol 11 (12) ◽

pp. 1651-1660

Author(s):

Lingfeng Xu ◽

Zhuoxuan Lu ◽

Guang-Hong Tan ◽

Feng-Ying Huang ◽

Rong Cao ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Blood Compatibility ◽

Leukemia Cell ◽

Leukemia Cells ◽

Mouse Serum ◽

G1 Arrest ◽

Normal Cells ◽

Leukemia Treatment

Leukemia is a group of blood cancers which seriously endangers the health of many people, especially children and adolescents. Although some drugs have been developed to treat leukemia, these drugs always have harmful side effects, which seriously affect the quality of life of patients. Therefore, the development of a special drug which damages only leukemia cells and does not harm normal cells remains a challenge. In a previous study, we developed a novel nanomedicine, Cy5.5MSA-G250, which selectively kills fast-growing tumor cells without harming normal cells. Based on our previous work, we prepared Cy5.5-HSA-G250 nanoparticles (CHGNPs) by replacing mouse serum albumin (MSA) with low immunogenic human serum albumin (HSA), and then applied this nanomaterial in leukemia treatment. Under physiological conditions, the CHGNPs exhibited good dispersion and stability, and hemolytic experiments showed that this material has excellent blood compatibility. The cell endocytosis of CHGNPs was obviously inhibited after treatment with nystatin and chlorpromazine, implying that caveolae-mediated endocytosis and clathrin-mediated endocytosis are involved in the cellular uptake of CHGNPs. Cytotoxicity and apoptosis assays revealed that the CHGNPs severely inhibited leukemia cell proliferation and induced leukemia cell apoptosis but did not affect normal cells. The selective up-regulation of tumor suppressor protein P27 and inducement of G1 arrest in leukemia cells may be the main mechanisms for CHGNPs' selective cytotoxicity. Owing to these advantages of CHGNPs, we believe that CHGNPs can be used as a potential leukemia drug for clinical treatment.

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Effects of human serum albumin complexed with free fatty acids on cell viability and insulin secretion in the hamster pancreatic β-cell line HIT-T15

Life Sciences ◽

10.1016/j.lfs.2011.02.022 ◽

2011 ◽

Vol 88 (17-18) ◽

pp. 810-818 ◽

Cited By ~ 8

Author(s):

Vivian C. Tuei ◽

Ji-Sook Ha ◽

Chung-Eun Ha

Keyword(s):

Fatty Acids ◽

Insulin Secretion ◽

Human Serum Albumin ◽

Serum Albumin ◽

Cell Viability ◽

Free Fatty Acids ◽

Human Serum ◽

Cell Line ◽

Pancreatic Β Cell ◽

Β Cell

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Biological effect and molecular docking of anticancer palladium and platinum complexes with morpholine dithiocarbamate on human serum albumin as a blood carrier protein

Canadian Journal of Physiology and Pharmacology ◽

10.1139/cjpp-2017-0693 ◽

2018 ◽

Vol 96 (12) ◽

pp. 1276-1285 ◽

Cited By ~ 2

Author(s):

Seyed Ali Hosseini ◽

Mahboube Eslami Moghadam ◽

Maryam Saeidifar ◽

Ali Akbar Saboury

Keyword(s):

Molecular Docking ◽

Circular Dichroism ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Myelogenous Leukemia ◽

Leukemia Cell Line ◽

Diffusion Method ◽

Spectroscopic Techniques ◽

Circular Dichroïsm

The aim of this study was to examine the interaction of [Pd(2,2′-bipyridine) (morpholinedithiocarbamate)]NO3 and [Pt (2,2′-bipyridine)(morpholinedithiocarbamate)]NO3 with human serum albumin under physiological conditions by using fluorescence, absorption, and circular dichroism spectroscopic techniques. Spectroscopic analysis of the emission quenching at different temperatures demonstrated that the quenching mechanism was static quenching. From the circular dichroism results, thermal stability study, it was found that the interaction of the complexes with human serum albumin caused a conformational change of the protein reversibly. These 2 anticancer Pd and Pt complexes were activated against chronic myelogenous leukemia cell line K562, so that 50% cytotoxic concentration values of 16 and 26 μM for Pd and Pt complexes, respectively, were observed, which were much lower than that of cisplatin (154 μM). Biological activities of both Pd and Pt complexes were also assayed against selective microorganisms by the disc diffusion method. These results showed that the Pd(II) complex is antifungal agent but Pt(II) complex has antibacterial activity. Also, the interaction of both metal derivative complexes was studied by molecular docking. Complementary molecular docking results may be useful to determine the binding mechanism of human serum albumin in pharmaceutical and biophysical studies providing new insight in the novel pharmacology.

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