Purpose: Bovine serum albumin (BSA) has been employed as a mild biological template in nanoscale particles. Copper sulfide (CuS) has been used for photothermal therapy (PTT) in several studies. In this study, we aimed to synthesize the 131 I-labeled BSA-modified CuS nanoparticles (131 I-BSA@CuS), with attributes of both radiotherapy and PTT, as a therapeutic agent against anaplastic thyroid carcinoma (ATC).
Method: BSA@CuS nanoparticles were prepared using the solvothermal reaction and then labeled with Na131 I by the chloramine-T method. The products were characterized and their cytotoxicity was investigated in vitro and in vivo. The therapeutic efficacy of 131 I-BSA@CuS was evaluated in ARO cell (an ATC cell line) subcutaneous tumors.
Results: The nanoparticles showed good biocompatibility and low toxicity in vitro and in vivo. BSA@CuS rapidly and effectively converted the light energy from an 808 nm laser into thermal energy with a conversion efficiency of 28.07%. SPECT/CT imaging demonstrated that the accumulation of radioactivity peaked within 24 h and resided in the tumors for 5 days post intratumoral injection. In vivo assays indicated that, compared to monotherapy, the synthesized nanoparticles employing both PTT and radiotherapy possess better therapeutic efficacy against tumors.
Conclusion: The synthesized nanomaterial showed uniform dispersion, good stability and aqueous solubility, excellent photothermal properties, and long-term retention in ATC. Hence, combined radiotherapy and PTT can significantly inhibit tumor growth compared to monotherapy, and can be applied in clinical settings.
Burkholderia pseudomallei pathogenesis in human skin fibroblasts: A Bsa type III secretion system is involved in the invasion, multinucleated giant cell formation, and cellular damage
Burkholderia pseudomallei-a causative agent of melioidosis that is endemic in Southeast Asia and Northern Australia-is a Gram-negative bacterium transmitted to humans via inhalation, inoculation through skin abrasions, and ingestion. Melioidosis causes a range of clinical presentations including skin infection, pneumonia, and septicemia. Despite skin infection being one of the clinical symptoms of melioidosis, the pathogenesis of B. pseudomallei in skin fibroblasts has not yet been elucidated. In this study, we investigated B. pseudomallei pathogenesis in the HFF-1 human skin fibroblasts.
On the basis of co-culture assays between different B. pseudomallei clinical strains and the HFF-1 human skin fibroblasts, we found that all B. pseudomallei strains have the ability to mediate invasion, intracellular replication, and multinucleated giant cell (MNGC) formation. Furthermore, all strains showed a significant increase in cytotoxicity in human fibroblasts, which coincides with the augmented expression of matrix metalloproteinase-2. Using B. pseudomallei mutants, we showed that the B. pseudomallei Bsa type III secretion system (T3SS) contributes to skin fibroblast pathogenesis, but O-polysaccharide, capsular polysaccharide, and short-chain dehydrogenase metabolism do not play a role in this process. Taken together, our findings reveal a probable connection for the Bsa T3SS in B. pseudomallei infection of skin fibroblasts, and this may be linked to the pathogenesis of cutaneous melioidosis.
Adenosine/A1R signaling pathway did not play dominant roles on the influence of SGLT2 inhibitor in the kidney of BSA-overloaded STZ-induced diabetic mice
Aims/introduction: A sodium glucose cotransporter 2 inhibitor (SGLT2i) has shown to display excellent renoprotective effects in DKD with macroalbuminuria/proteinuria. Regarding the renoprotective mechanism of SGLT2i, a sophisticated hypothesis was made by explaining the suppression of glomerular hypertension/hyperfiltration via the adenosine/adenosine type 1 receptor (A1R) signaling-mediated restoration of the tubulo-glomerular feedback mechanism; however, such A1R signaling is relevant for renoprotection by SGLT2i in DKD with proteinuria has not been elucidated.
Materials and methods: STZ induced diabetic CD-1 mice were injected with bovine serum albumin (BSA) and treated with SGLT2i in the presence/absence of AIR inhibitor administration.
Results: We found that the influences of SGLT2i are essentially independent of the activation of A1R signaling in the kidney of BSA-overloaded streptozotocin-induced diabetic mice. BSA-overloaded diabetic mice displayed trend of kidney damage with higher glomerular filtration (GFR) and the significant induction of fibrogenic genes such as transforming growth factor (TGF)- β2 and collagen type III (COL3). SGLT2i TA-1887 suppressed diabetes-induced GFR in BSA-overloaded diabetic mice associated with the significant suppression of TGF-β2 and COL3; A1R-specific inhibitor 8-cyclopentyl-1,3-dipropylxanthine (DPCPX) did not cancel the effects of TA-1887 on either GFR or associated gene levels. Both TA-1887 and DPCPX-treated BSA-overloaded diabetic mice displayed suppressed HbA1c levels associated with the increased food intake. When analyzing the association among histological evaluation, GFR and potential fibrogenic gene levels, each group of mice displayed distinct correlation patterns.
Conclusions: A1R signaling activation was not the dominant mechanism on the influence of SGLT2 inhibitor in the kidney of BSA-overloaded diabetic mice.
Mixed Ni(II) and Co(II) complexes of nalidixic acid drug: Synthesis, characterization, DNA/BSA binding profile and in vitro cytotoxic evaluation against MDA-MB-231 and HepG2 cancer cell lines
In this work, herein we report the synthesis, structural characterization and in vitro cytotoxic evaluation of two mixed Co(II)/Ni(II)-nalidixic acid-bipyridyl complexes (1 and 2). The structural analysis of metal complexes 1 and 2 was carried out by analytical and multispectroscopic techniques (FT-IR, UV-vis, EPR, sXRD). The crystallographic details of complexes 1 and 2 revealed a monoclinic crystal system with P21/c space group. DFT studies of complexes were performed to get electronic structure and localization of HOMO and LUMO electron densities. Hirshfeld surface analysis of metal complexes 1 and 2 was employed to understand the various intermolecular interactions (C-H···O, N-H···H and O-H···O) that define the stability of crystal lattice structures.
The comparative interaction studies of complex 1 and complex 2 with DNA/BSA were performed by diverse multispectroscopic and analytical techniques to evaluate their chemotherapeutic potential. The magnitude of the DNA binding propensity and binding mode was verified by calculating Kb, K and Ksv values. Higher binding affinity was observed in case of complex 2via intercalative mode. Furthermore, the cytotoxic assessment of complexes 1 and 2 was examined against MDA-MB-231 (triple negative human breast cancer cell line) and HepG2 (liver carcinoma cell line) employing MTT assay which revealed remarkably effecient and specific cytotoxic activity of complex 2.
BSA |
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31C-CH0114 | Fitzgerald | 50 mg | 95 EUR |
BSA |
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E8M0809-3 | EnoGene | 100ul | 275 EUR |
BSA |
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MBS5303530-50mg | MyBiosource | 50mg | 200 EUR |
BSA |
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MBS5303530-5x50mg | MyBiosource | 5x50mg | 740 EUR |
BSA |
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MBS2567134-10g | MyBiosource | 10g | 150 EUR |
BSA |
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MBS2567134-50g | MyBiosource | 50g | 340 EUR |
BSA |
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MBS2567134-5g | MyBiosource | 5g | 125 EUR |
BSA |
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MBS2567134-5x50g | MyBiosource | 5x50g | 1490 EUR |
BSA |
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pro-422 | ProSpec Tany | 10gr | 140 EUR |
Testosterone 3 BSA Protein (BSA) |
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abx060856-100g | Abbexa | 100 µg | Ask for price |
Testosterone 3 BSA Protein (BSA) |
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abx060856-10g | Abbexa | 10 µg | 837.5 EUR |
Testosterone 3 BSA Protein (BSA) |
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abx060856-1mg | Abbexa | 1 mg | 693.6 EUR |
Testosterone 3 BSA Protein (BSA) |
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abx060856-50g | Abbexa | 50 µg | Ask for price |
Native BSA Bovine Serum Albumin (BSA) |
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MBS2124008-001mg | MyBiosource | 0.01mg | 85 EUR |
Native BSA Bovine Serum Albumin (BSA) |
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MBS2124008-005mg | MyBiosource | 0.05mg | 110 EUR |
Native BSA Bovine Serum Albumin (BSA) |
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MBS2124008-01mg | MyBiosource | 0.1mg | 125 EUR |
Native BSA Bovine Serum Albumin (BSA) |
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MBS2124008-02mg | MyBiosource | 0.2mg | 135 EUR |
Native BSA Bovine Serum Albumin (BSA) |
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MBS2124008-05mg | MyBiosource | 0.5mg | 185 EUR |
BSA Control for AGE-BSA |
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35R-AA007 | Fitzgerald | 10 mg | Ask for price |
BSA Control for Age-BSA |
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2221-BSA | Biovision | each | 210 EUR |
BSA 30% |
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IBS-BB006a | iNtRON Biotechnology Inc | 5 mL | 140 EUR |
Albumin, Human Serum (BSA) (BSA & Azide Free) |
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MBS6120698-025mg | MyBiosource | 0.25(mg | 445 EUR |
Albumin, Human Serum (BSA) (BSA & Azide Free) |
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MBS6120698-1mg | MyBiosource | 1mg | 1015 EUR |
Albumin, Human Serum (BSA) (BSA & Azide Free) |
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MBS6120698-5x1mg | MyBiosource | 5x1mg | 4415 EUR |
THC (BSA) |
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abx080017-1mg | Abbexa | 1 mg | 510 EUR |
SAH (BSA) |
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abx083009-100l | Abbexa | 100 µl | 575 EUR |
SAH (BSA) |
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abx083009-1ml | Abbexa | 1 ml | Ask for price |
SAH (BSA) |
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abx083009-200l | Abbexa | 200 µl | Ask for price |
SAH (BSA) |
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abx083009-50ug | Abbexa | 50 ug | 460.8 EUR |
PCP [BSA] |
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DAG3015 | Creative Diagnostics | 1 mg | 656.25 EUR |
Probing the interaction of new and biologically active Pd(II) complex with DNA/BSA via joint experimental and computational studies along with thermodynamic, NLO, FMO and NBO analysis
- Treatment with transition metal complexes is an efficient method to fight with cancer. Therefore, a new transition metal complex formulated as [Pd(1, 3-pn)(acac)]Cl (pn and acac stand for propylendiamine and acetylacetonate, respectively) was synthesized and analyzed using 1H NMR, Fourier transform infrared, electronic absorption spectroscopy techniques as well as elemental analysis and conductivity measurement. The geometry optimization, frontier molecular orbital (FMO) analysis, molecular electrostatic potential (MEP), natural bond orbital (NBO) analysis and nonlinear optical (NLO) property were accomplished by density functional theory (DFT) at B3LYP level with 6-311G(d,p)/aug-cc-pVTZ-PP basis set.
- Preliminary determination of antitumor activity and lipophilicity of this metal complex was performed experimentally and the promising results were obtained. This encouraged us to study the interaction and binding mode/modes of this complex with DNA as the primary receptor for the chemotropic drugs and BSA as the transporter protein in the circulatory system.
- For this reason, the binding of newly made complex was assessed in-vitro under physiological state using experimental and in-silico molecular modeling studies. So, the CT-DNA binding study of this complex was explored using spectrofluorometric as well as spectrophotometric techniques, viscosity and gel electrophoresis experiments. Furthermore, fluorescence, UV-Vis, F[Formula: see text]rster resonance energy transfer and circular dichroism studies were carried out for BSA binding. The experimental and computational interaction studies showed that [Pd(1, 3-pn)(acac)]Cl complex binds to the minor groove of CT-DNA and interacts with BSA by van der Waals forces and hydrogen bond.