Carboxymethyl Cellulose Hydrogel Based Formulations of Zinc Hydroxide Nitrate-Sodium Dodecylsulphate-Bispyribac Nanocomposite: Advancements in Controlled Release Formulation of Herbicide

2021 ◽  
Vol 21 (12) ◽  
pp. 5867-5880
Author(s):  
Sharifah Norain Mohd Sharif ◽  
Norhayati Hashim ◽  
Illyas Md Isa ◽  
Suriani Abu Bakar ◽  
Mohamad Idris Saidin ◽  
...  
Keyword(s):  
Controlled Release ◽  
Aqueous Solutions ◽  
Carboxymethyl Cellulose ◽  
Matrix Material ◽  
Release Time ◽  
Zinc Hydroxide ◽  
Dependent Manner ◽  
Diffusion Kinetic ◽  
Concentration Dependent Manner ◽  
Release Formulation

The usefulness of carboxymethyl cellulose (CMC) as a matrix material in enhancing the controlled release formulations of bispyribac (BP) herbicide from the interlayer gallery of zinc hydroxide nitratesodium dodecylsulphate–bispyribac (ZHN–SDS–BP) nanocomposite was investigated. The CMC coated nanocomposite, ZHN–SDS–BP–CMC was characterised using several instruments for the determination of its physicochemical properties. The release rates of the BP were measured using a UV spectrophotometer, and the aqueous solutions containing PO3−4 , SO2−4 and Cl− were selected as release media in the release studies so as to mimic the real conditions of environmental soil. Significant release time delays, triggered by the gelation forming ability and hygroscopic nature of CMC, were observed in all release media, and the release processes were found to behave in a concentration-dependent manner in all release media. Fitting the release data into several kinetic models demonstrated that release in aqueous solutions of Na3PO4 and Na2SO4 was governed by pseudo second order processes, whereas the release in an aqueous NaCl solution was governed by the parabolic diffusion kinetic model. The potential of CMC in prolonging the release of BP from ZHN–SDS–BP–CMC can potentially help in reducing the pollution resulting from the overuse of pesticides.

Synthesis, controlled release and antibacterial studies of nalidixic acid–zinc hydroxide nitrate nanocomposites

2016 ◽  
Vol 40 (1) ◽  
pp. 238-244 ◽  
Author(s):  
Hafezeh Nabipour ◽  
Moayad Hossaini Sadr ◽  
Nygil Thomas
Keyword(s):  
Controlled Release ◽  
Nalidixic Acid ◽  
Antibacterial Agent ◽  
Zinc Hydroxide ◽  
Release Formulation ◽  
Antibacterial Studies ◽  
Controlled Release Formulation ◽  
Zinc Hydroxide Nitrate

Nalidixic acid intercalated zinc hydroxide nitrate is suitable for a controlled-release formulation and the resultant nanocomposite is an effective antibacterial agent.

scholarly journals Colloidal solution of silver nanoparticles for label-free colorimetric sensing of ammonia in aqueous solutions

2018 ◽  
Vol 9 ◽  
pp. 499-507 ◽  
Author(s):  
Alessandro Buccolieri ◽  
Antonio Serra ◽  
Gabriele Giancane ◽  
Daniela Manno
Keyword(s):  
Silver Nanoparticles ◽  
Aqueous Solutions ◽  
Morphological Analysis ◽  
Colloidal Solution ◽  
Ammonia Concentration ◽  
Dependent Manner ◽  
Label Free ◽  
Colorimetric Sensing ◽  
Concentration Dependent Manner ◽  
High Ammonia

Silver nanoparticles were synthesized in the presence of saccharides and ammonia (NH3) in the concentration range from 10−2 to 103 ppm to develop an optical sensor for NH3 in aqueous solutions. Ammonia affects the features of the nanoparticles obtained in a concentration-dependent manner as determined by UV–vis absorption analysis and TEM observations. Structural and morphological analysis provides the basis for the production of a colorimetric label-free sensor for ammonia. Overall, surface plasmon resonance increases when ammonia concentration rises, although the functional trend is not the same over the entire investigated ammonia concentration range. Three different ranges have been identified: very low ammonia concentrations from 0.01 to 0.2 ppm, high ammonia concentrations from 20 to 350 ppm and, most importantly, the intermediate or physiological range of ammonia from 0.5 to 10 ppm.

Adsolubilisation of thiacloprid pesticide into the layered zinc hydroxide salt intercalated with dodecyl sulphate, for controlled release formulation

2019 ◽  
Vol 24 (5) ◽  
pp. 279-288 ◽  
Author(s):  
Zuhailimuna Muda ◽  
Norhayati Hashim ◽  
Illyas Md Isa ◽  
Suzaliza Mustafar ◽  
Suriani Abu Bakar ◽  
...  
Keyword(s):  
Controlled Release ◽  
Zinc Hydroxide ◽  
Release Formulation ◽  
Controlled Release Formulation ◽  
Layered Zinc Hydroxide

The Anti-Atherogenic Properties of Sesamin are Mediated via Improved Macrophage Cholesterol Efflux Through PPARγ1-LXRα and MAPK Signaling

2014 ◽  
Vol 84 (1-2) ◽  
pp. 79-91 ◽  
Author(s):  
Amin F. Majdalawieh ◽  
Hyo-Sung Ro
Keyword(s):  
Cholesterol Efflux ◽  
Transcriptional Activity ◽  
Molecular Mechanisms ◽  
Foam Cell ◽  
Mapk Signaling ◽  
Luciferase Reporter ◽  
Foam Cell Formation ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Macrophage Cholesterol Efflux

Background: Foam cell formation resulting from disrupted macrophage cholesterol efflux, which is triggered by PPARγ1 and LXRα, is a hallmark of atherosclerosis. Sesamin and sesame oil exert anti-atherogenic effects in vivo. However, the exact molecular mechanisms underlying such effects are not fully understood. Aim: This study examines the potential effects of sesamin (0, 25, 50, 75, 100 μM) on PPARγ1 and LXRα expression and transcriptional activity as well as macrophage cholesterol efflux. Methods: PPARγ1 and LXRα expression and transcriptional activity are assessed by luciferase reporter assays. Macrophage cholesterol efflux is evaluated by ApoAI-specific cholesterol efflux assays. Results: The 50 μM, 75 μM, and 100 μM concentrations of sesamin up-regulated the expression of PPARγ1 (p< 0.001, p < 0.001, p < 0.001, respectively) and LXRα (p = 0.002, p < 0.001, p < 0.001, respectively) in a concentration-dependent manner. Moreover, 75 μM and 100 μM concentrations of sesamin led to 5.2-fold (p < 0.001) and 6.0-fold (p<0.001) increases in PPAR transcriptional activity and 3.9-fold (p< 0.001) and 4.2-fold (p < 0.001) increases in LXR transcriptional activity, respectively, in a concentration- and time-dependent manner via MAPK signaling. Consistently, 50 μM, 75 μM, and 100 μM concentrations of sesamin improved macrophage cholesterol efflux by 2.7-fold (p < 0.001), 4.2-fold (p < 0.001), and 4.2-fold (p < 0.001), respectively, via MAPK signaling. Conclusion: Our findings shed light on the molecular mechanism(s) underlying sesamin’s anti-atherogenic effects, which seem to be due, at least in part, to its ability to up-regulate PPARγ1 and LXRα expression and transcriptional activity, improving macrophage cholesterol efflux. We anticipate that sesamin may be used as a therapeutic agent for treating atherosclerosis.

Neutrophil Elastase Potentiates Cathepsin G-lnduced Platelet Activation

1992 ◽  
Vol 68 (05) ◽  
pp. 570-576 ◽  
Author(s):  
Mary A Selak
Keyword(s):  
Neutrophil Elastase ◽  
Cell Activation ◽  
Thromboxane A2 ◽  
Creatine Phosphate ◽  
Dense Granule ◽  
Cathepsin G ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Low Concentrations ◽  
High Concentrations

SummaryWe have previously demonstrated that human neutrophil cathepsin G is a strong platelet agonist that binds to a specific receptor. This work describes the effect of neutrophil elastase on cathepsin G-induced platelet responses. While platelets were not activated by high concentrations of neutrophil elastase by itself, elastase enhanced aggregation, secretion and calcium mobilization induced by low concentrations of cathepsin G. Platelet aggregation and secretion were potentiated in a concentration-dependent manner by neutrophil elastase with maximal responses observable at 200 nM. Enhancement was observed when elastase was preincubated with platelets for time intervals of 10–60 s prior to addition of a low concentration of cathepsin G and required catalytically-active elastase since phenylmethanesulphonyl fluoride-inhibited enzyme failed to potentiate cell activation. Neutrophil elastase potentiation of platelet responses induced by low concentrations of cathepsin G was markedly inhibited by creatine phosphate/creatine phosphokinase and/or indomethacin, indicating that the synergism between elastase and cathepsin G required the participation of ADP and thromboxane A2. On the other hand, platelet responses were not attenuated by the PAF antagonist BN 52021, signifying that PAF-acether did not play a role in elastase potentiation. At higher concentrations porcine pancreatic elastase exhibits similar effects to neutrophil elastase, demonstrating that the effect of elastase was not unique to the neutrophil protease. While neutrophil elastase failed to alter the ability of cathepsin G to hydrolyze a synthetic chromogenic substrate, preincubation of platelets with elastase increased the apparent affinity of cathepsin G binding to platelets. In contrast to their effect on cathepsin G-induced platelet responses, neither neutrophil nor pancreatic elasatse potentiated aggregation or dense granule release initiated by ADP, PAF-acether, arachidonic acid or U46619, a thromboxane A2 mimetic. Moreover, unlike its effect on cathepsin G, neutrophil elastase inhibited thrombin-induced responses. The current observations demonstrate that elastase can potentiate platelet responses mediated by low concentrations of cathepsin G, suggesting that both enzymes may function synergistically to activate platelets under conditions where neutrophil degranulation occurs.

Trimucytin: A Collagen-Like Aggregating Inducer Isolated from Trimeresurus mucrosquamatus Snake Venom

1993 ◽  
Vol 69 (03) ◽  
pp. 286-292 ◽  
Author(s):  
Che-Ming Teng ◽  
Feng-Nien Ko ◽  
Inn-Ho Tsai ◽  
Man-Ling Hung ◽  
Tur-Fu Huang
Keyword(s):  
Platelet Aggregation ◽  
Snake Venom ◽  
Inositol Phosphate ◽  
Shape Change ◽  
Platelet Activating Factor ◽  
Atp Release ◽  
Platelet Membrane ◽  
Thromboxane B2 ◽  
Dependent Manner ◽  
Concentration Dependent Manner

SummaryTrimucytin is a potent platelet aggregation inducer isolated from Trimeresurus mucrosquamatus snake venom. Similar to collagen, trimucytin has a run of (Gly-Pro-X) repeats at the N-terminal amino acids sequence. It induced platelet aggregation, ATP release and thromboxane formation in rabbit platelets in a concentration-dependent manner. The aggregation was not due to released ADP since it was not suppressed by creatine phosphate/creatine phosphokinase. It was not either due to thromboxane A2 formation because indomethacin and BW755C did not have any effect on the aggregation even thromboxane B2 formation was completely abolished by indomethacin. Platelet-activating factor (PAF) was not involved in the aggregation since a PAF antagonist, kadsurenone, did not affect. However, RGD-containing peptide triflavin inhibited the aggregation, but not the release of ATP, of platelets induced by trimucytin. Indomethacin, mepacrine, prostaglandin E1 and tetracaine inhibited the thromboxane B2 formation of platelets caused by collagen and trimucytin. Forskolin and sodium nitroprusside inhibited both platelet aggregation and ATP release, but not the shape change induced by trimucytin. In quin-2 loaded platelets, the rise of intracellular calcium concentration caused by trimucytin was decreased by 12-O-tetradecanoyl phorbol-13 acetate, imipramine, TMB-8 and indomethacin. In the absence of extracellular calcium, both collagen and trimucytin caused no thromboxane B2 formation, but still induced ATP release which was completely blocked by R 59022. Inositol phosphate formation in platelets was markedly enhanced by trimucytin and collagen. MAB1988, an antibody against platelet membrane glycoprotein Ia, inhibited trimucytinand collagen-induced platelet aggregation and ATP release. However, trimucytin did not replace the binding of 125I-labeled MAB1988 to platelets. Platelets pre-exposed to trimucytin were resistant to the second challenge with trimucytin itself or collagen. It is concluded that trimucytin may activate collagen receptors on platelet membrane, and cause aggregation and release mainly through phospholipase C-phosphoinositide pathway.

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