44 research outputs found

    Exploration of natural polymers for use as green corrosion inhibitors for AZ31 magnesium alloy in saline environment

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    Seven natural polymers namely, chitosan (CHI), dextran (Dex), carboxymethyl cellulose (CMC), sodium alginate (ALG), pectin (PEC), hydroxylethyl cellulose (HEC), and Gum Arabic (GA) were screened for anticorrosion property towards AZ31 Mg alloy in 3.5 wt.% NaCl solution. CHI, Dex, CMC, PEC, and GA accelerated the corrosion while ALG and HEC moderately inhibited the corrosion of the alloy. HEC and ALG (1 g/L) protected the alloy by 64.13 % and 58.27 %, respectively. Two inhibitor cocktails consisting of either HEC or ALG, KI, and Date palm seed oil have been formulated. HEC- and ALG-formulations inhibited the alloy corrosion by 80.56 % and 77.43 %, respectively from EIS technique. Surface observation studies using SECM, AFM, SEM, and EDX agreed with other experimental results revealing effective corrosion inhibition by the formulations. X-ray photoelectron spectroscopy, FTIR, and UV–vis results disclose that Mg(OH)2 co-existed with adsorbed inhibitor complexes

    Recent insights in nanotechnology-based drugs and formulations designed for effective anti-cancer therapy

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    Interleukin 13 Mutants of Enhanced Avidity Toward the Glioma-Associated Receptor, IL13Rα2

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    Interleukin 13 (IL13) binds a receptor that is highly overexpressed in malignant gliomas, IL13Rα2. IL13 protein is composed of four helices: α-helix A, B, C, and D, and we found a new “hot spot” in α-helix D that is crucial for the binding of IL13 to IL13Rα2. Lys-105 plus Lys-106 and Arg-109 represent this hot spot. In the current study, we have made substitutions at these three positions in IL13. We examined both neutralization of an IL13-based cytotoxin's glioma cell killing and direct receptor binding of the new IL13 mutants. We observed that Lys-105 and Arg-109 are critical for IL13 binding to IL13Rα2, indeed. However, new mutants of important properties were identified with regard to tumor targeting. IL13.K105R mutant, in which lysine was substituted by arginine, neutralized the killing of IL13Rα2-positive cells by IL13-based cytotoxin more efficiently than wild-type IL13. However, IL13.K105L or IL13.K105A was deprived of any such activity. Furthermore, IL13.K105R and IL13.R109K competed 77- and 27-fold better, respectively, with the binding of [(125)I]IL13 to the IL13Rα2 binding sites when compared with wild-type IL13. Thus, we have uncovered the first forms of IL13 of higher avidity toward IL13Rα2. These mutants should prove useful in the further design of anticancer diagnostics/therapeutics

    Serum chemistry analysis.

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    <p>The analysis was performed 48 hours post injection of the 7mg/kg dose of targeted and non-targeted liposomal doxorubicin. The values were compared with control mice injected with phosphate buffered saline. The levels indicate that liver functional enzymes including bilirubin and alkaline phosphatase are comparable in both the treated and control groups of mice. Creatinine and BUN levels are also comparable to that of untreated control mice, indicating that renal function is not significantly affected due to treatment.</p

    IL13Rα2 expression in various tissues from a peripheral nerve carcinoma tissue microarray.

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    <p>Representative microscopic images from the tissue microarray after IHC for IL13Rα2 expression are shown (panel A-F). Malignant Schwannoma distinctly shows robust expression of IL13Rα2 in the tissue (D) with positive expression in benign neurofibromas as evident from the IHC (E,F). Normal nerve tissue indicated minimal staining without distinct cellular morphology. No IL13Rα2 staining was observed in cancer adjacent normal tissues.</p
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