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antiviral agent
A substance that destroys or inhibits replication of viruses.
anti-HIV agent
An antiviral agent that destroys or inhibits the replication of the human immunodeficiency virus.
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anticoagulant
An agent that prevents blood clotting.
antiatherosclerotic agent
A cardiovascular drug that prevents atherosclerosis (a disease in which the inside of an artery narrows due to the build up of plaque). Compare with antiatherogenic agent. |
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View more via ChEBI Ontology
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Dextran polysulfate
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ChemIDplus
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Dextran sulfate
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KEGG COMPOUND
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Dextran sulfate 500
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ChemIDplus
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Dextran sulfuric acid
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ChemIDplus
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Dextran sulfuric acid ester
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ChemIDplus
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Dextran sulphate
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ChemIDplus
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Polydextran sulfate
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ChemIDplus
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8187464
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Beilstein Registry Number
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Beilstein
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9042-14-2
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CAS Registry Number
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ChemIDplus
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Yu C, Liu H, Guo C, Chen Q, Su Y, Guo H, Hou X, Zhao F, Fan H, Xu H, Zhao Y, Mu X, Wang G, Xu H, Chen D (2022)
Dextran sulfate-based MMP-2 enzyme-sensitive SR-A receptor targeting nanomicelles for the treatment of rheumatoid arthritis.
Drug delivery 29, 454-465 [PubMed:35119317]
[show Abstract]
Rheumatoid arthritis (RA) is an ordinarily occurring autoimmune disease with systemic inflammatory. Targeted drug delivery systems have many successful applications in the treatment of rheumatoid arthritis. In order to develop nanoparticles for targeted delivery of Celastrol (Cel) to rheumatoid arthritis and specific drug release, the dextran sulfate (DS) was modified as the targeting molecular by binding to the scavenger receptor of macrophage. The dextran-sulfate-PVGLIG-celastrol (DS-PVGLIG-Cel), named DPC, amphiphilic polymeric prodrug was synthesized and characterized. The resulting DPC@Cel micelles had the average size of 189.9 nm. Moreover, the micelles had ultrahigh entrapment efficiency (about 44.04%) and zeta potential of -11.91 mV. In the in vitro release study, due to the excessive production of matrix metalloproteinase-2 (MMP-2) at the inflammatory joint, the MMP-2 reactive peptide was used to crack in the inflammatory microenvironment to accelerate the release of Cel. The results have shown that the nanoparticles can effectively deliver Cel to activated macrophages and significantly improve the bioavailability. In vivo experiments showed that DPC@Cel have better anti-rheumatoid arthritis effects and lower systemic toxicity than free Cel. This study provided a new therapeutic strategy for the treatment of RA. | Shen K, Long J, Li X, Hua Y, Chen Y, Kong X, Zhang C (2022)
Complexation of pea protein isolate with dextran sulphate and interfacial adsorption behaviour and O/W emulsion stability at acidic conditions
International journal of food science & technology. 57, 2333-2345 [Agricola:IND607703858]
[show Abstract]
This study was aimed at improving the emulsifying property and physical stability of pea protein isolate (PPI) stabilised emulsions at acidic conditions by complexation with dextran sulphate (DS). Soluble and insoluble complexes with different charge and particle size were formed depending on the phase separation behaviour. The surface adsorption of PPI became slower after complexation with DS, but the percentage of adsorbed proteins at the oil–water interface was not affected. The formation of PPI–DS soluble complexes at high content of DS (≥0.4%) significantly improved the negative net charges of PPI, prevented the aggregation of protein, which further improved the emulsifying property of PPI at acidic conditions through the strong electrostatic repulsion and steric hindrance effects. Insoluble complexes with relatively weak net charge and large particles were formed at low DS content (≤0.2%), resulting in the bridging flocculation of oil droplets at pH 5 and 4. Thus, the emulsifying ability of PPI under acidic conditions could be significantly improved by formation of soluble complexes with DS. | Fuse T, Nakagaki T, Homma T, Tange H, Yamaguchi N, Atarashi R, Ishibashi D, Nishida N (2021)
Dextran sulphate inhibits an association of prions with plasma membrane at the early phase of infection.
Neuroscience research 171, 34-40 [PubMed:33476681]
[show Abstract]
The defining characteristic of prion diseases is conversion of a cellular prion protein (PrPC) to an abnormal prion protein (PrPSc). The exogenous attachment of PrPSc to the surface of a target cell is critical for infection. However, the initial interaction of PrPSc with the cell surface is poorly characterized. In the current study, we specifically focused on the association of PrPSc with cells during the early phase of infection, using an acute infection model. First, we treated mouse neuroblastoma N2a-58 cells with prion strain 22 L-infected brain homogenates and revealed that PrPSc was associated with membrane fractions within three hours, a short exposure time. These results were also observed in PrPC-deficient hippocampus cell lines. We also demonstrate here that PrPSc from 22 L-infected brain homogenates was associated with lipid rafts during the early phase of infection. Furthermore, we revealed that DS500, a glycosaminoglycan mimetic, inhibited both the attachment of PrPSc to membrane fractions and subsequent prion transmission, suggesting that the early association of prions with cell surface is important for prion infection. | Ammassam Veettil R, Marcano DC, Yuan X, Zaheer M, Adumbumkulath A, Lee R, Isenhart LC, Soriano N, Mhatre K, Joseph R, Mani SA, Shin CS, Acharya G (2021)
Dextran Sulfate Polymer Wafer Promotes Corneal Wound Healing.
Pharmaceutics 13, 1628 [PubMed:34683921]
[show Abstract]
Eye injuries due to corneal abrasions, chemical spills, penetrating wounds, and microbial infections cause corneal scarring and opacification that result in impaired vision or blindness. However, presently available eye drop formulations of anti-inflammatory and antibiotic drugs are not effective due to their rapid clearance from the ocular surface or due to drug-related side effects such as cataract formation or increased intraocular pressure. In this article, we presented the development of a dextran sulfate-based polymer wafer (DS-wafer) for the effective modulation of inflammation and fibrosis and demonstrated its efficacy in two corneal injury models: corneal abrasion mouse model and alkali induced ocular burn mouse model. The DS-wafers were fabricated by the electrospinning method. We assessed the efficacy of the DS-wafer by light microscopy, qPCR, confocal fluorescence imaging, and histopathological analysis. These studies demonstrated that the DS-wafer treatment is significantly effective in modulating corneal inflammation and fibrosis and inhibited corneal scarring and opacification compared to the unsulfated dextran-wafer treated and untreated corneas. Furthermore, these studies have demonstrated the efficacy of dextran sulfate as an anti-inflammatory and antifibrotic polymer therapeutic. | Spirig R, van Kooten C, Obregon C, Nicod L, Daha M, Rieben R (2008)
The complement inhibitor low molecular weight dextran sulfate prevents TLR4-induced phenotypic and functional maturation of human dendritic cells.
Journal of immunology (Baltimore, Md. : 1950) 181, 878-890 [PubMed:18606639]
[show Abstract]
Low molecular weight dextran sulfate (DXS) has been reported to inhibit the classical, alternative pathway as well as the mannan-binding lectin pathway of the complement system. Furthermore, it acts as an endothelial cell protectant inhibiting complement-mediated endothelial cell damage. Endothelial cells are covered with a layer of heparan sulfate (HS), which is rapidly released under conditions of inflammation and tissue injury. Soluble HS induces maturation of dendritic cells (DC) via TLR4. In this study, we show the inhibitory effect of DXS on human DC maturation. DXS significantly prevents phenotypic maturation of monocyte-derived DC and peripheral myeloid DC by inhibiting the up-regulation of CD40, CD80, CD83, CD86, ICAM-1, and HLA-DR and down-regulates DC-SIGN in response to HS or exogenous TLR ligands. DXS also inhibits the functional maturation of DC as demonstrated by reduced T cell proliferation, and strongly impairs secretion of the proinflammatory mediators IL-1beta, IL-6, IL-12p70, and TNF-alpha. Exposure to DXS leads to a reduced production of the complement component C1q and a decreased phagocytic activity, whereas C3 secretion is increased. Moreover, DXS was found to inhibit phosphorylation of IkappaB-alpha and activation of NF-kappaB. These findings suggest that DXS prevents TLR-induced maturation of human DC and may therefore be a useful reagent to impede the link between innate and adaptive immunity. | Spirig R, Gajanayake T, Korsgren O, Nilsson B, Rieben R (2008)
Low molecular weight dextran sulfate as complement inhibitor and cytoprotectant in solid organ and islet transplantation.
Molecular immunology 45, 4084-4094 [PubMed:18722664]
[show Abstract]
Complement is an essential part of the innate immune system and plays a crucial role in organ and islet transplantation. Its activation, triggered for example by ischemia/reperfusion (I/R), significantly influences graft survival, and blocking of complement by inhibitors has been shown to attenuate I/R injury. Another player of innate immunity are the dendritic cells (DC), which form an important link between innate and adaptive immunity. DC are relevant in the induction of an immune response as well as in the maintenance of tolerance. Modulation or inhibition of both components, complement and DC, may be crucial to improve the clinical outcome of solid organ as well as islet transplantation. Low molecular weight dextran sulfate (DXS), a well-known complement inhibitor, has been shown to prevent complement-mediated damage of the donor graft endothelium and is thus acting as an endothelial protectant. In this review we will discuss the evidence for this cytoprotective effect of DXS and also highlight recent data which show that DXS inhibits the maturation of human DC. Taken together the available data suggest that DXS may be a useful reagent to prevent the activation of innate immunity, both in solid organ and islet transplantation. | Chen Y, Huang H, Yu X, Qi L (2005)
Chiral recognition of dextran sulfate with D- and L-cystine studied by multiwavelength surface plasmon resonance.
Carbohydrate research 340, 2024-2029 [PubMed:16002055]
[show Abstract]
A multiwavelength surface plasmon resonance (mwSPR) approach has been developed to study the chiral discrimination between D- and L-cystine (Cys). A monolayer of the two enantiomers was separately assembled on a pair of gold films of about 50 nm in thickness and their resonance wavelength shifts, Deltalambda, were measured under a continuous flow of an identical chiral probe solution. Dextran sulfate (DS) was found to be an excellent chiral probe because it has rich chiral centers and is large enough to produce sensitive mwSPR response. The chiral discrimination was investigated either by Deltalambda(max), the maximum resonance wavelength shift in recognition equilibrium, or by recognition kinetics (Deltalambda vs time). The equilibrium data showed that D-Cys yielded always the smaller Deltalambda(max) as compared to L-Cys at pH 5.0 or above. This differentiation was enlarged by raising the probe content and became naught at pH <4.5. The kinetic results showed that, as pH increased from 5.0 to 7.5, the non-equilibrium Deltalambda for D-Cys rose above the level for L-Cys at the first 30s of recognition but came back gradually to its equilibrium position after about 150 s, with crossing at 50--150 s depending on DS concentration. This phenomenon was thought to be the result of molecular orientation adjustment after DS binding to D-Cys. Both kinetic and thermodynamic mechanisms were thus considered to be deeply involved in the investigated chiral recognition system. | Tiyaboonchai W, Woiszwillo J, Middaugh CR (2003)
Formulation and characterization of DNA-polyethylenimine-dextran sulfate nanoparticles.
European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences 19, 191-202 [PubMed:12885383]
[show Abstract]
Polyethylenimine (PEI) is a promising non-viral gene delivery polymer that produces high transfection efficiency both in vitro and in vivo. The use of PEI, however, is hindered by its toxicity, reflecting its polycationic nature. In an attempt to decrease this charge-dependent cytotoxicity, a polyanionic polymer, dextran sulfate (DS), has been incorporated into self-assembling PEI-DNA complexes with zinc as stabilizing agent. Spherical particles with a mean particle size of approximately 200 nm and a polydispersity index of 0.2 were achieved using the following optimal conditions: PEI solutions at pH 8, PEI/DS mass ratios of >or=2, and 25 microM zinc sulfate. Plasmid DNA was completely condensed within the nanoparticles as confirmed by an ethidium bromide accessibility assay. This result correlates well with DNase protection studies which find partial protection of the DNA nanoparticles from degradation by the enzyme. The DNA was incorporated into the PEI-DS particles with a high efficiency (>95%) and maintained a primarily supercoiled B-form as determined by gel electrophoresis and circular dichroism. The cytotoxicity of the DNA nanoparticles appeared to decrease as the amount of DS in the formulation was increased and they produced moderate transfection activities that were only modestly inhibited by the presence of serum. | Tokita S, Arai M, Yamamoto N, Katagiri Y, Tanoue K, Igarashi K, Umeda M, Inoue K (1996)
Specific cross-reaction of IgG anti-phospholipid antibody with platelet glycoprotein IIIa.
Thrombosis and haemostasis 75, 168-174 [PubMed:8713797]
[show Abstract]
To study the pathological functions of anti-phospholipid (anti-PL) antibodies, we have analyzed their effect on platelet function. We identified an IgG anti-PL mAb, designated PSG3, which cross-reacted specifically with glycoprotein (GP) IIIa in human platelets and inhibited platelet aggregation. PSG3 bound also to certain polyanionic substances, such as double-stranded DNA, heparan sulfate, dextran sulfate and acetylated-LDL, but not to other polyanionic substances. The binding of PSG3 to GPIIIa was completely inhibited by heparan sulfate and dextran sulfate, indicating that PSG3 recognizes a particular array of negative charges expressed on both GPIIIa and the specified polyanionic substances. Since neither neuraminidase- nor endoglycopeptidase F-treatment of GPIIIa had any significant effect on the binding of PSG3, this array must be located within the amino acid sequence of GPIIIa but not in the carbohydrate moiety. Reduction of the disulfide bonds in GPIIIa greatly reduced its reactivity, suggesting that the negative charges in the epitope are arranged in a particular conformation. PSG3 inhibited platelet aggregation induced by either ADP or collagen, it also inhibited fibrinogen binding to activated platelets in a dose-dependent fashion. PSG3, however, did not inhibit the binding of GRGDSP peptide to activated platelets. These results suggest that the PSG3 epitope on GPIIIa contains a particular array of negative charges, and possibly affects the fibrinogen binding to GPIIb/IIIa complex necessary for platelet aggregation. | Tsubamoto Y, Yamada N, Watanabe Y, Inaba T, Shiomi M, Shimano H, Gotoda T, Harada K, Shimada M, Ohsuga J (1994)
Dextran sulfate, a competitive inhibitor for scavenger receptor, prevents the progression of atherosclerosis in Watanabe heritable hyperlipidemic rabbits.
Atherosclerosis 106, 43-50 [PubMed:8018106]
[show Abstract]
Dextran sulfate competes with binding of modified LDL to the scavenger receptor in macrophages. To elucidate the role of dextran sulfate in the atherosclerotic process, 100 mg of dextran sulfate in drinking water was given to 5 Watanabe heritable hyperlipidemic (WHHL) rabbits for 12 months starting at age 4 months. During the experimental period, there were no significant differences in plasma cholesterol levels between dextran sulfate-treated and untreated rabbits. After 12 months' treatment, accumulation of cholesterol ester in total aorta was significantly suppressed in dextran sulfate-treated rabbits as compared with untreated rabbits (71.4 +/- 22.3 vs. 42.7 +/- 16.5 mg/g dry weight, P < 0.05). Furthermore, lesion area with atherosclerotic plaques in treated rabbits was significantly less than that in untreated rabbits (59.7 +/- 24.5 vs. 30.4 +/- 14.4%, P < 0.05). These results indicate that dextran sulfate might prevent the progression of atherosclerosis by competitively inhibiting the binding of modified LDL to scavenger receptors. | Nakashima H, Yoshida O, Baba M, De Clercq E, Yamamoto N (1989)
Anti-HIV activity of dextran sulphate as determined under different experimental conditions.
Antiviral research 11, 233-246 [PubMed:2478075]
[show Abstract]
Dextran sulphate is a potent and selective inhibitor of human immunodeficiency virus type 1 (HIV-1). Its anti-HIV-1 activity has been investigated under varying experimental conditions. MT-4 cells were infected with HIV-1 at different multiplicities of infection (MOI), and treated with either dextran sulphate, 3'-azido-2',3'-dideoxythymidine (AZT), or anti-HIV-1 serum obtained from an ARC patient. Dextran sulphate suppressed HIV-1 replication (as monitored by viral antigen expression) when the MOI was 0.01 or 0.1. It was ineffective at an MOI of 1.0. The anti-HIV-1 serum was only partially effective at an MOI of 0.01 and ineffective at an MOI of 0.1 or 1.0. AZT proved effective at all three MOIs. Co-cultures of uninfected and HIV-1-infected MT-4 cells were protected against destruction by dextran sulphate at a concentration of 10 and 100 micrograms/ml. To fully suppress viral antigen expression a concentration of 100 micrograms/ml was needed. When used at this concentration, a 1-h contact of dextran sulphate with the cells during the virus adsorption period sufficed to suppress HIV-1 antigen expression. In this sense, dextran sulphate behaved like the anti-HIV-1 serum. Dextran sulphate also behaved like OKT-4A in that they both inhibited HIV-1 attachment to the MT-4 cells, whereas OKT-4 failed to do so. However, dextran sulphate did not affect the binding of OKT-4A to the cells. The present results support the concept that dextran sulphate owes its anti-HIV-1 activity mainly to inhibition of virus binding to its target cells. The anti-HIV-1 activity of dextran sulphate is highly dependent on its sulphate content. | GRASSET E, SCHWARTZ DE (1954)
[Inhibition of coagulant principles in snake venoms by dextran sulfate, a synthetic anticoagulant of bacterial origin].
Schweizerische Zeitschrift fur Pathologie und Bakteriologie. Revue suisse de pathologie et de bacteriologie 17, 514-520 [PubMed:13225707] |
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