> Chemicals & Drugs > Organic Chemical > Suramin

Suramin

Q: What are some common usage challenges with Suramin?

Suramin can have a range of side effects, including nephrotoxicity, neurotoxicity, and coagulopathy. Researchers need to be mindful of dosage levels and monitor patients closely when using Suramin in clinical trials or other applications. Additionally, Suramin has limited solubility, which can pose formulation challenges for certain delivery methods.

Suramin is a synthetic polysulfonated napththylurea compound with a wide range of biological activities.
It has been used as an antiparasitic drug, particularly for the treatment of African trypanosomiasis and onchocerciasis.
Suramin also exhibits antiviral, antineoplastic, and anticoagulant properties, and has been investigateed for its potential in treating various cancers, HIV infection, and other diseases.
Researchers can use PubCompare.ai's AI-driven platform to locate the best protocols and products for Suramin research by comparing data across literature, preprints, and patents, optimizing their studies and unlocking new insights.

Most cited protocols related to «Suramin»

Behavioral Assessment of Autistic-like Traits

Cited 24 times

Behavioral testing began at 13 weeks of age, after 1 month of weekly antipurinergic therapy with suramin. Mice were tested in social approach, T-maze, locomomtor activity, marble burying, acoustic startle, and prepulse inhibition paradigms as follows. The ages at the time of testing are noted in the figure legends. For a complete description of the behavioral paradigms see Full Methods Online. Social Preference and Social Novelty. Social behavior was tested as social preference as previously described
[9 (link)], with the addition of a third phase with a second novel mouse to interrogate social novelty
[19 (link)]. T-Maze. Novelty preference was tested as spontaneous alternation behavior in the T-maze as previously described
[9 (link)]. Marble Burying. Marble burying behavior was measured over 30 min by a modification of methods used by Thomas et al.[20 (link)]. Locomotor Activity. Locomotor activity, hyperactivity (total distance traveled), center entries, holepoke exploration, and vertical investigation (rearing) behaviors were quantified by automated beam break analysis in the mouse behavioral pattern monitor (mBPM) as previously described
[21 (link)]. Acoustic Startle and Prepulse Inhibition. Sensitivity to acoustic startle and prepulse inhibition of the startle reflex were measured by automated testing in commercial startle chambers as previously described
[22 (link)].

Naviaux J.C., Wang L., Li K., Bright A.T., Alaynick W.A., Williams K.R., Powell S.B, & Naviaux R.K. (2015). Antipurinergic therapy corrects the autism-like features in the Fragile X (Fmr1 knockout) mouse model. Molecular Autism, 6, 1.

Full text: Click here

Publication 2015

Acoustics Hypersensitivity Locomotion Marble MAZE protocol Mice, House Prepulse Inhibition Reflex, Moro Suramin Therapeutics

Live Imaging of Microglial Dynamics

Cited 9 times

CX3CR1^+/GFP animals were euthanized and their eyes immediately enucleated and immersed in oxygenated Ringer's solution containing (in mM): 125 NaCl, 5 KCl, 1.5 CaCl₂, 0.75 MgCl₂/6 H₂O, 1.25 NaH₂PO₄, 10 D-glucose, 20 HEPES (pH 7.35–7.45). Retinas were dissected free from the eyecup and flat-mounted on black Millipore filter paper (HABP045; Millipore, Billerica, MA) with the ganglion cell layer facing upwards. Flat-mount retinal explants were maintained in Ringer's solution at room temperature in a humidified, oxygenated chamber for no longer than 6 hours after dissection. For imaging experiments, explants were transferred to a stage-mounted, temperature-controlled (32°C) chamber (Bioptechs, Butler, PA) through which oxygenated Ringer's solution was continuously superfused. GFP-labeled microglia were imaged using a confocal microscope (SP2; Leica, Exton, PA) and a 40× (0.80 numerical aperture) water-immersion objective. Multiplane Z-series time-lapse images spanning the dimensions of imaged microglia were collected at a 512×512 pixel resolution at a rate of one image stack every 10 seconds. Agonists and antagonists were administered by superfusion into the recording chamber. Microglial morphology and motility were evaluated before, during, and after superfusion of each agent. The duration of a typical recording was approximately 25–33 minutes (150–200 image stacks). Neurotransmitter agonists evaluated were: AMPA, kainate, NMDA (all from Tocris), glutamate, GABA, and ATP (all from Sigma). Antagonists evaluated were: NBQX (1,2,3,4-tetrahydro-6-nitro-2,3-dioxo-benzo[f]quinoxaline-7-sulfonamide disodium) a kainate/AMPA receptor antagonist; GYKI-52466, an AMPA receptor antagonist; APV (2-amino-5-phosphonopentanoic acid), an NMDA receptor antagonist; bicuculline, a ionotropic GABA_A receptor antagonist; suramin, a broad-spectrum P2 receptor antagonist (all from Tocris Bioscience, Ellisville, MO). Apyrase (Sigma, St. Louis, MO), an enzyme catalyzing the hydrolysis of ATP, was also evaluated.

Fontainhas A.M., Wang M., Liang K.J., Chen S., Mettu P., Damani M., Fariss R.N., Li W, & Wong W.T. (2011). Microglial Morphology and Dynamic Behavior Is Regulated by Ionotropic Glutamatergic and GABAergic Neurotransmission. PLoS ONE, 6(1), e15973.

Full text: Click here

Publication 2011

2,3-dioxo-6-nitro-7-sulfamoylbenzo(f)quinoxaline 2-Amino-5-phosphonovalerate agonists alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid AMPA Receptors Animals antagonists Apyrase Bicuculline Cells Dissection Enzymes Eye GABA-A Receptor Antagonists gamma Aminobutyric Acid Ganglia Glucose Glutamate GYKI 52466 HEPES Hydrolysis Kainate Magnesium Chloride Microglia Microscopy, Confocal Motility, Cell N-Methyl-D-Aspartate Receptors N-Methylaspartate Neoplasm Metastasis Neurotransmitters Quinoxalines Receptors, Kainic Acid Retina Ringer's Solution Sodium Chloride Submersion Sulfonamides Suramin

Diagnosis and Treatment of HAT in Uganda

Cited 7 times

Patients with HAT and non-infected control individuals presenting to local hospitals or identified during community surveillance were recruited in Eastern Uganda in 2002 and 2003. The Tororo, Iganga, Jinja and Busia Districts define a common ecotope for the transmission by Glossina fuscipes fuscipes of T.b.rhodesiense which will be referred to henceforth as the Tororo focus, while the Soroti District contains a separate G.f.fuscipes ecotope where HAT emerged as a new epidemic in 1998/9 [11 (link)]. Diagnosis was by microscopic detection of trypanosomes in wet blood films, giemsa stained thick blood films or in the buffy coat fraction after microhematocrit centrifugation [12 (link)]. Following admission, a detailed physical examination was performed and neurological involvement was assessed using the Glasgow Coma Score (GCS) [13 (link)]. The GCS gives a measure of the degree of impairment of consciousness, with a score of 15 as normal. The ranges 14-12, 11-8, < 8, indicate mild, moderate and severe impairment of consciousness respectively. A clinical history was taken either from the patient or the attendant relative, and patients were classified on the basis of language to either Bantu, Western- or Eastern-Nilotic ethnic groups [14 ]. Stage determination was by examination of cerebrospinal fluid (CSF) using the WHO criteria in which patients with trypanosomes in the CSF and/or a cell count >5cells/mm³ were classified as late stage [15 (link)]. Early stage infection was treated with suramin and late stage infection with melarsoprol [9 (link)]. Subjects or their guardians signed consent forms after receiving standard information in their local language. Protocols were approved by the Grampian Research Ethics Committee (Aberdeen) and the Ministry of Health (Uganda). Malaria-parasitemic and microfilaremic individuals were excluded from the study.
Blood samples taken before treatment commenced were collected into EDTA-vacutainers (Greiner, Stroud, UK) and centrifuged for 10 minutes at 3000g. Platelet-depleted plasma was aliquoted and frozen immediately in liquid nitrogen. CSF samples taken as part of normal stage diagnosis were also frozen and stored in liquid nitrogen. Trypanosome DNA from a subset of cases was sampled by applying a 200μl suspension taken from the buffy coat layer to FTA cards (Whatman Bioscience, Maidstone, UK), which were dried and stored at room temperature. Cases were selected to include representatives from each village and no more than one case per compound/family.

MacLean L., Odiit M., MacLeod A., Morrison L., Sweeney L., Cooper A., Kennedy P.G, & Sternberg J.M. (2007). SPATIALLY AND GENETICALLY DISTINCT AFRICAN TRYPANOSOME VIRULENCE VARIANTS DEFINED BY HOST-INTERFERON-GAMMA RESPONSE. The Journal of infectious diseases, 196(11), 1620-1628.

Publication 2007

BLOOD Blood Platelets Centrifugation Cerebrospinal Fluid Comatose Consciousness Diagnosis Edetic Acid Epidemics Ethics Committees, Research Ethnic Groups Freezing Glossina Infection Legal Guardians Malaria Melarsoprol Microscopy Nitrogen Patients Physical Examination Plasma Stain, Giemsa Suramin Transmission, Communicable Disease Trypanosoma

Crystallographic Studies of Wild-Type and Variant G6PD Enzymes

Cited 5 times

Crystals of WT G6PD recombinant enzyme grew in sitting drops containing 20% w/v PEG 3350, 0.2 M potassium formate, pH 7.3. Suramin (G6PD inhibitor) was added to the protein solution (the final concentration in the drop was 0.5 mM) prior to the crystallization. Canton G6PD recombinant enzyme was crystallized in sitting drops containing 20% w/v PEG 3350, 0.2 M ammonium citrate tribasic, pH 7.0. AG1 dissolved in 30% DMSO was added to the protein prior to the crystallization to reach final concentration of 0.5 mM in the drop. None of the Suramin or AG1 compound was visible in the electron density map of WT G6PD and Canton G6PD; however, they significantly improved diffracting quality of the crystals. Note that our inability to observe AG1 in the crystal structure may reflect instability or flexibility of the ligand bound to G6PD. Additional crystallographic studies and further medicinal chemistry efforts will help determine the binding site of AG1 in the enzyme and the mechanism by which it activates G6PD. X-ray diffraction data of WT G6PD and Canton G6PD were collected at 100 K at beamline 12–2 of Stanford Synchrotron Radiation Light Source (SSRL) and beamline 5.0.2 of Advanced Light Source (ALS), respectively. A solution of 20% glycerol was used as cryo-protectant. Crystals of WT and Canton G6PD diffracted to 1.9 Å and 2.6 Å resolution, respectively. The data were processed using iMOSFLM⁵⁷, and further analysis of the data by POINTLESS^{58 (link),59 (link)} indicated the space group of F222 and P2₁2₁2₁ for WT G6PD and Canton G6PD crystals, respectively. WT G6PD structure was solved using molecular replacement with a monomeric G6PD structure from PDB: 2BHL used as a search model in MOLREP. Canton G6PD structure was solved using the WT G6PD structure that was already solved in this study. Molecular models were further built in Coot^{60 (link)}. Both structures were refined using the restrained isotropic refinement in REFMAC^{61 (link),62 (link)}. TLS parameters were not used for the refinement in both cases. Each refinement was done using 10 cycles of maximum likelihood restrained refinement, with geometry weight adjusted to 0.05. Data collection and refinement statistics are summarized in Table 1. The atomic coordinates and structure factors are deposited in the PDB database under accession codes PDB: 6E08 for WT G6PD and PDB: 6E07 for Canton G6PD. All structure figures were prepared using PyMOL (PyMOL Molecular Graphics System, Version 1.5.0.5; Schrödinger).

Hwang S., Mruk K., Rahighi S., Raub A.G., Chen C.H., Dorn L.E., Horikoshi N., Wakatsuki S., Chen J.K, & Mochly-Rosen D. (2018). Correcting glucose-6-phosphate dehydrogenase deficiency with a small-molecule activator. Nature Communications, 9, 4045.

Full text: Click here

Publication 2018

ammonium citrate Binding Sites Crystallization Crystallography Electrons Enzymes formic acid, potassium salt Glucosephosphate Dehydrogenase Glycerin Ligands Light Molecular Structure polyethylene glycol 3350 Protective Agents Proteins Radiation Sulfoxide, Dimethyl Suramin X-Ray Diffraction

Visualizing Intracellular Na+ Distribution

Cited 5 times

To evaluate the effects of eATP on the pattern of intracellular Na⁺ distribution, we used a Na⁺-specific fluorescent dye, CoroNa-Green AM, to visualize Na⁺ within cells [40] (link). After the treatments were applied in Series 1 and 3, suspended cells were loaded with CoroNa-Green AM (20 µM) for 2 h and analyzed with confocal microscopy. The confocal settings were as follows: excitation 488 nm, emission 510–530 nm, frame 512×512. The Na⁺-specific fluorescence in the cytosolic and vacuolar compartments were calculated with Image-Pro Plus 6.0 software (Media Cybernetics, Bethesda, USA). In addition to the effects of long-term salt stress (24 h), we also examined the effects of suramin, PPADS, and H-G on Na⁺ compartmentation after a short-term treatment (1 h, Series 2).

Sun J., Zhang X., Deng S., Zhang C., Wang M., Ding M., Zhao R., Shen X., Zhou X., Lu C, & Chen S. (2012). Extracellular ATP Signaling Is Mediated by H2O2 and Cytosolic Ca2+ in the Salt Response of Populus euphratica Cells. PLoS ONE, 7(12), e53136.

Full text: Click here

Publication 2012

Cells Cytosol Fluorescence Fluorescent Dyes Longterm Effects Microscopy, Confocal Protoplasm pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid Reading Frames Salt Stress Suramin Vacuole

Most recents protocols related to «Suramin»

Tau Liquid-Liquid Phase Separation Dynamics

The trDLS experiments were performed with solutions of 25 µM Tau, 50 μg/ml to 100 μg/ml polyA, 0.85 µM or 5 µM heparin, and 25 to 100 µM suramin. The solutions were prepared at a two-fold concentration and centrifuged for 15 min at 16000 g at room temperature prior to trDLS experiments. To induce Tau LLPS, polyA or suramin were added to Tau in a DLS cuvette in concentrations mentioned above and trDLS measurements and data acquisition was carried out using a Spectroscatter-301 (Xtal Concepts, Germany) equipped with a laser providing a wavelength of 660 nm. Sample solutions were measured at a fixed 90° scattering angle in quartz-glass cuvettes (path length: 1.5 mm, Hellma Analytics, Müllheim, Germany) at 20 °C. The trDLS experiments were performed three times to confirm the reproducibility of the data. The obtained autocorrelation functions (ACFs) of each experiment were averaged over 20 seconds for each data point. Averaged ACFs were fitted by applying the CONTIN regularization software^{62 (link)}, and corresponding hydrodynamic radii, R_h, were calculated via the Stokes–Einstein equation,

R_{h} = \frac{k_{B} T}{6 π η D}

with k_B being the Boltzmann constant, T the temperature, η the viscosity, and D_t the diffusion constant. The polydispersity index (PDI) is a measure of the size heterogeneity in a sample. Polydispersity can also occur due to agglomeration or aggregation in the sample. PDI values were calculated based on a nonlinear statistical method of the CONTIN software, where the maximum value for a monodispersed sample is 20%. The PDI for only monodispersed Tau before they form condensates are indicated at the onset of the DLS experiment. In short, PDIs were derived using the Xtal Concepts algorithm with the

k_{2} / {\bar{Γ}}^{2}

relationship, where Γ is the decay constant and is directly related to the diffusion behaviour of macromolecules (Dτ), whereas

\bar{Γ}

is the mean of Γ values and k₂ is the variance of measured distributions for the decay rates of the Gaussian distribution^{63 (link),64 (link)}.

Prince P.R., Hochmair J., Brognaro H., Gevorgyan S., Franck M., Schubert R., Lorenzen K., Yazici S., Mandelkow E., Wegmann S, & Betzel C. (2023). Initiation and modulation of Tau protein phase separation by the drug suramin. Scientific Reports, 13, 3963.

Full text: Click here

Publication 2023

Diffusion Genetic Heterogeneity Heparin Hydrodynamics Neoplasm Metastasis Poly A Quartz Radius Suramin Viscosity

Tau Binding Affinity Measurement by MST

To measure the binding affinity of suramin with Tau in the condensates, we performed an MST experiment using Tau labelled with RED-MALEIMIDE 2nd Generation (Cysteine Reactive). In brief, Tau at 140 nM was co-incubated with suramin at different concentrations ranging from 153 nM to 5 mM and the fluorescence signal was recorded for around 20 s after laser-induced heating. The analysis of MST data and graph plots were prepared by Thermo Affinity online tool developed by eSPC facilty of EMBL^{68 (link)} and MO.Affinity Analysis v2.3 (Nano Temper) software provided by the manufacturer (Supplementary Fig. S2a).

Full text: Click here

Publication 2023

Cysteine Fluorescence maleimide Suramin

Tau Condensates FRAP Imaging

Tau:suramin condensates containing 2% DyLight-488 labeled Tau (labeled using amine-reactive DyLight488-NHS ester (Thermo Scientific) following manufacturer instructions) were imaged before and directly after bleaching with a 488 nm laser (90% intensity; 6 loops). The recovery of the fluorescence in the bleached region (circular ROIs, diameter 1 to 2 µm), a similar non-bleached reference-ROI (inside a different condensate) and a background ROI (Region of interest) were monitored in parallel for 40 s. FRAP curves were background corrected and normalized to the background corrected reference signal. Experiments were performed at room temperature on a spinning disk confocal microscope (Eclipse-Ti CSU-X, Nikon) using a 60x oil objective (Fig. 1g).

Full text: Click here

Publication 2023

Amines Esters Fluorescence Microscopy, Confocal Suramin

Tau:Suramin Condensates Visualization by TEM

For TEM experiments of Tau:suramin condensates (Fig. 1i), the Tau:suramin samples were prepared in the similar way as applied for DLS experiments in equimolar concentrations for Tau (25 µM) and suramin (25 µM) and 5 µM for heparin. About 3 µl of undiluted sample was loaded onto glow discharged carbon-coated copper grids, (Quantifoil R 1.2/1.3, Science Services), incubated for 30 seconds to allow adherence of condensates, blotted to remove excess solution, stained with 2% (w/v) uranyl acetate (UA) solution for 15 seconds and dried as per the standard negative staining protocol for proteins to reduce background and increase contrast. The morphology and dimensions of Tau:suramin condensates were analyzed by TEM (JEM-2100-Plus, JEOL, Germany) and micrographs were taken at an accelerating voltage of 200 kV. All TEM experiments were conducted in the XBI Biolab of European XFEL^{65 (link)}. The experiments were repeated three times. For Tau TEM fibril investigations the Tau:suramin, Tau:heparin and Tau:suramin:heparin condensate samples were prepared and incubated at 37 °C for 36 hours along with suramin control (Fig. 4c).

Full text: Click here

Publication 2023

Carbon Copper Europeans Heparin Neoplasm Metastasis Proteins Suramin uranyl acetate

Tau Protein Condensates Formation

To induce condensates, if not indicated differently final concentration of 25 µM suramin (Sigma-S2671; 1,429.17 g/mol, 1.4 kDa) and/or 0.85 to 5 µM heparin (Applichem; 8–25 kDa and MP Biomedicals-101931; 17–19 kDa) and/or 50 μg/ml polyA RNA (Sigma-P9403; MW 385.3) were added to 25 µM Tau diluted in 25 mM HEPES (pH 7.4), 10 mM NaCl, 1 mM DTT. All Tau condensates for DLS were prepared at room temperature and nuclease-free water was used for all buffers. The Tau condensates were imaged 1–2 h after formation by adding 2.5 µl of the solution onto an amine-treated glass-bottom dish (TC-treated Miltenyi, GC 1.5). The dish was closed and equipped with a ddH2O prewetted tissue at the inner edges to avoid evaporation. Imaging was performed on a widefield microscope (Eclipse-Ti, Nikon) using a 60x oil or 40x water objective. The rest of the samples were incubated at 37 °C for 24 h and used in the HEK sensor cell assay.

Full text: Click here

Publication 2023

Amines Biological Assay Buffers Cells Heparin HEPES Hyperostosis, Diffuse Idiopathic Skeletal Microscopy RNA, Polyadenylated Sodium Chloride Suramin Tissues

Top products related to «Suramin»

Suramin by Merck Group

Sourced in United States, Germany, Australia, Japan

Suramin is a laboratory chemical compound that functions as an inhibitor of various enzymes and biological processes. It is commonly used in research applications to study the mechanisms and effects of enzyme inhibition. Suramin exhibits a broad range of biological activities, making it a versatile tool for scientific investigations.

Adenosine triphosphate (atp) by Merck Group

Sourced in United States, Germany, United Kingdom, China, Sao Tome and Principe, Italy, Japan, Macao, Spain, Canada, France, Switzerland, Ireland, Sweden, Australia

ATP is a laboratory instrument used to measure the presence and concentration of adenosine triphosphate (ATP) in various samples. ATP is a key molecule involved in energy transfer within living cells. The ATP product provides a reliable and accurate method for quantifying ATP levels, which is useful in applications such as microbial detection, cell viability assessment, and ATP-based assays.

Apyrase by Merck Group

Sourced in United States, United Kingdom, Germany, Japan, France, Macao, Sao Tome and Principe

Apyrase is an enzyme that catalyzes the hydrolysis of ATP and ADP to AMP and inorganic phosphate. It is commonly used in various biochemical and cell biology applications.

Suramin by Bio-Techne

Sourced in United Kingdom, United States

Suramin is a lab equipment product manufactured by Bio-Techne. It is a synthetic polysulfonated naphthylurea compound that functions as a competitive antagonist of various growth factors and enzymes. Suramin can inhibit the activities of certain proteins involved in cellular processes. The core function of Suramin is to act as a research tool for studying the effects of growth factor and enzyme inhibition in in vitro and in vivo experimental settings.

Ppads by Bio-Techne

Sourced in United Kingdom, United States

PPADS is a receptor antagonist that selectively binds to P2X receptors. It is commonly used in research applications to study the role of P2X receptors in various biological processes.

Adenosine by Merck Group

Sourced in United States, Germany, United Kingdom, China, Sao Tome and Principe, France, Italy, Austria, Canada, Japan, Switzerland

Adenosine is a laboratory chemical used for various research and analytical applications. It is a naturally occurring nucleoside composed of adenine and ribose. Adenosine plays a role in cellular energy transfer and signaling processes. Due to its versatile properties, Adenosine is a widely used compound in many scientific fields.

Adenosine diphosphate (adp) by Merck Group

Sourced in United States, United Kingdom, Germany, China, Sao Tome and Principe, France, Spain, Italy, Macao, Switzerland

ADP is a high-performance liquid chromatography (HPLC) system designed for analytical and preparative separations. It features advanced technology to deliver precise and reproducible results. The core function of ADP is to facilitate the separation, identification, and purification of complex mixtures of chemical compounds.

Carbenoxolone by Merck Group

Sourced in United States, Germany, United Kingdom, France

Carbenoxolone is a laboratory product manufactured by Merck Group. It is a chemical compound used in research applications, though its specific core function is not provided in order to maintain an unbiased and factual approach.

Mrs2500 by Bio-Techne

Sourced in United States, United Kingdom

The MRS2500 is a laboratory instrument designed for the accurate measurement of refractive index. It utilizes the Abbe refractometer principle to determine the refractive index of liquids, gels, and solid samples. The instrument provides precise and reliable refractive index measurements across a wide range of sample types.

Fluo 4 am by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Germany, Canada, China, France, Spain, Italy, Sweden, Japan, Switzerland, Belgium, Australia, Austria, Finland, New Zealand

Fluo-4 AM is a fluorescent calcium indicator used for the detection and measurement of intracellular calcium levels. It functions by binding to calcium ions, which results in an increase in fluorescence intensity. This product is commonly used in various cell-based assays and research applications involving calcium signaling.

What is Suramin and what are its key properties?

Suramin is a synthetic polysulfonated naphthylurea compound with a wide range of biological activities. It has been used as an antiparasitic drug, particularly for the treatment of African trypanosomiasis and onchocerciasis. Suramin also exhibits antiviral, antineoplastic, and anticoagulant properties, and has been investigated for its potential in treating various cancers, HIV infection, and other diseases.

How can PubCompare.ai help with Suramin research?

PubCompare.ai allows you to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform can help researchers identify the most effective protocols related to Suramin for their specific research goals. PubCompare.ai's AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accurecy.

What are some common usage challenges with Suramin?

Are there different variations or types of Suramin?

While Suramin is a single chemical entity, there are some variations in how it is synthesized and formulated. For example, some researchers have explored liposomal or nanoparticle-encapsulated forms of Suramin to improve solubility and targeted delivery. There may also be differences in purity or specific manufacturing processes that can impact the properties and performance of Suramin samples.

What are some of the key applications of Suramin?

In addition to its use as an antiparasitic drug, Suramin has been investigated for its potential in treating various cancers, viral infections (including HIV), and other diseases. Researchers have explored Suramin's antiangiogenic, antiproliferative, and anticoagulant effects, which could make it useful for applications like inhibiting tumor growth, preventing metastasis, and managing coagulation disorders.

More about "Suramin"

Suramin is a synthetic polysulfonated naphthylurea compound with a wide range of biological activities.
It has been utilized as an antiparasitic medication, particularly for the treatment of African trypanosomiasis (sleeping sickness) and onchocerciasis (river blindness).
Suramin also exhibits antiviral, antineoplastic (anti-cancer), and anticoagulant properties, and has been investigated for its potential in treating various malignancies, HIV infection, and other diseases.
Researchers can leverage PubCompare.ai's AI-driven platform to locate the best protocols and products for Suramin-related research by comparing data across academic literature, preprints, and patents.
This optimization can help enhance the reproducibility and accuracy of Suramin studies, unlocking new insights.
Suramin's mechanism of action involves interference with the activities of various enzymes, such as ATPases, apyrases, and purinergic (P2) receptors like P2X and P2Y.
It can inhibit the actions of ATP, ADP, and adenosine, as well as modulate the effects of PPADS (pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid) and carbenoxolone.
Suramin may also impact cellular calcium signaling through its interactions with Fluo-4 AM, a calcium indicator dye.
By exploring the wealth of information available on Suramin and related compounds, researchers can design more effective and informed studies, leading to breakthroughs in the understanding and treatment of a wide range of diseases.