Tyloxapol 0.125% solution
Requires a prescription from a doctor or prescriber
Tyloxapol is a non-ionic detergent often used as a surfactant.
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1 branded products available
WHO defined daily dose (DDD)
5 mg
Not a recommended dose. The DDD is the assumed average maintenance dose per day for a drug used for its main indication in adults. It is a statistical measure used for research and comparison purposes only.
Source: WHO Collaborating Centre for Drug Statistics Methodology, distributed via the NHS dm+d supplementary BNF/ATC mapping files (NHSBSA). Contains public sector information licensed under the Open Government Licence v3.0.
Therapeutically similar medicines
Similarity is based on WHO Anatomical Therapeutic Chemical (ATC) classification and on a factual NHS dm+d therapeutic-grouping code prefix. Source data: NHS dm+d via TRUD (OGL v3.0), WHO ATC/DDD Index.
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SNOMED CT and dm+d codes from NHS TRUD (Technology Reference data Update Distribution), licensed under the Open Government Licence v3.0. BNF code shown is the factual mapping value distributed by NHS Business Services Authority (NHSBSA) in the dm+d supplementary file under OGL v3.0; it is not affiliated with, nor licensed from, the publishers of the British National Formulary. ATC codes from the WHO Collaborating Centre for Drug Statistics Methodology (whocc.no).
Active and completed clinical studies from ClinicalTrials.gov
Source: ClinicalTrials.gov, a database of the U.S. National Library of Medicine (NLM), National Institutes of Health (NIH). Data accessed via ClinicalTrials.gov API v2. Trial information is provided for research purposes and does not constitute medical advice.
Academic studies and reviews for this medicine's active substance
Showing all 24 studies.
Reviews & meta-analyses: 1 · 1999–2026
Showing all 24 studies, sorted by most relevant.
Yilin Zhao, Mi Jing, Fei Wang
BMC Pulmonary Medicine, 2026
This study aimed to compare the efficacy and safety of different mucolytic agents in patients with COPD. This study enrolled adults, regardless of the medication regimen. The control groups received placebo, usual care, or a medication other than the intervention group. We reported interleukin-6 (IL-6), interleukin-8 (IL-8), ROS, COPD Assessment Test (CAT) scores, forced expiratory volume in 1 s (FEV1), adverse effects, and exacerbation rates. Statistical analyses were performed using Stata MP15, R4.4.3, and Bayesian network models. The quality of the included studies was assessed using RoB 2.0. PubMed, Embase, Cochrane Library, and Web of Science were searched from database inception up to January 28, 2026 to identify English-language randomized controlled trials (RCTs) reporting outcomes related to inflammatory markers and pulmonary function parameters. The study protocol was registered with PROSPERO (CRD42024622223). Data from 4408 COPD patients across 18 RCTs were analyzed. For reducing 8-isoprostane (SUCRA was 97.06%) and ROS (SUCRA was75.26%), erdosteine 900 mg was more effective. Regarding inflammatory markers, tyloxapol outperformed in reducing IL-6 (SUCRA was 67.16%) and IL-8 levels (SUCRA was 69.44%). For improving FEV1, erdosteine 900 mg (SUCRA: 89.40%) ranked first according to the SUCRA ranking. For reducing exacerbation rates of COPD (SUCRA: 87.72%) and the incidence of adverse reactions (SUCRA: 79.04%), cineole was the most efficacious. These results demonstrated that cineole was the most favorable for lowering the incidence of adverse reactions and exacerbation. Erdosteine 900 mg is most effective for improving lung function and reducing oxidative stress, while cineole is safer with a lower incidence of adverse reaction and acute exacerbation. Future multicenter, large-sample RCTs are warranted to collect data on long-term safety, explore combination therapies, and systematically monitor adverse drug reactions.
Abstract licence: CC BY-NC-ND
Oren Regev, Raoul Zana
Journal of Colloid and Interface Science, 1999
S. Mehta, N. Jindal
Colloids and surfaces. B, Biointerfaces, 2013
- Absorption
- Antitubercular Agents
- Chemistry, Pharmaceutical
Ayşe Nurseli Sulumer, E. Palabıyık, Bahri Avcı, et al.
Biotechnology and Applied Biochemistry, 2023
- Butyrylcholinesterase
- Hyperlipidemias
- Polyethylene Glycols
X. Ji, Qianqian Ma, Xuan Wang, et al.
Journal of ethnopharmacology, 2023
- Dyslipidemias
- Lipids
- Liver
Shuya Masuda, Shiho Yano, Tomohisa Tadokoro, et al.
Journal of Pharmaceutical Health Care and Sciences, 2024
BACKGROUND: Brinzolamide (BRI) suspensions are used for the treatment of glaucoma; however, sufficient drug delivery to the target tissue after eye drop administration is hampered by poor solubility. To address this issue, we focused on nanocrystal technology, which is expected to improve the bioavailability of poor-solubility drugs, and investigated the effect of BRI nanocrystal formulations on corneal permeability and intraocular pressure (IOP)-reducing effect. METHODS: BRI nanocrystal formulations were prepared by the wet-milling method with beads and additives. The particle size was measured by NANOSIGHT LM10, and the morphology was determined using a scanning probe microscope (SPM-9700) and a scanning electron microscope (SEM). Corneal permeability was evaluated in vitro using a Franz diffusion cell with rat corneas and in vivo using rabbits, and the IOP-reducing effect was investigated using a rabbit hypertensive model. RESULTS: The particle size range for prepared BRI nanocrystal formulation was from 50 to 300 nm and the mean particle size was 135 ± 4 nm. The morphology was crystalline, and the nanoparticles were uniformly dispersed. In the corneal permeability study, BRI nanocrystallization exhibited higher corneal permeability than non-milled formulations. This result may be attributed to the increased solubility of BRI by nanocrystallization and the induction of energy-dependent endocytosis by the attachment of BRI nanoparticles to the cell membrane. Furthermore, the addition of tyloxapol to BRI nanocrystal formulation further improved the intraocular penetration of BRI and showed a stronger IOP-reducing effect than the commercial product. CONCLUSIONS: The combination of BRI nanocrystallization and tyloxapol is expected to be highly effective in glaucoma treatment and a useful tool for new ophthalmic drug delivery.
Abstract licence: CC BY
Jun‐Hui Choi, Se‐Eun Park, Seung Kim
eFood, 2024
Abstract Several previous research indicate that treating Mesembryanthemum crystallinum may aid in reducing adipogenesis and triacylglycerol level and improving hyperglycemia and diabetes. Therefore, the present study was designed to evaluate the effectiveness of M. crystallinum extract (MCE) in combating obesity and lowering fat/lipid/cholesterol levels. The study aimed to investigate the molecular docking model targeting 3‐hydroxy‐3‐methylglutaryl‐CoA reductase (HMGCR) using MCE‐derived d ‐pinitol or atorvastatin, an inhibitor of HMGCR. In this study, histological alterations in the liver of tyloxapol‐induced hyperlipidemia (TIH) model, hyperlipidemia‐related markers in serum, HMGCR activity, and cell viability in HepG2 cells were analyzed. Our findings revealed that tyloxapol treatment significantly led to increased hyperlipidemia‐related indicators and cardiovascular‐associated risk indices. However, MCE effectively mitigated tyloxapol‐induced hepatic fat accumulation and an increase in cholesterol levels. This was achieved through improvements in metabolic parameters, ultimately ameliorating TIH. These beneficial results suggest that MCE may be a strong potential for the treatment of hyperlipidemia‐related diseases.
Abstract licence: CC BY
Monique Opperman, R. Pietersen, D. Loots, et al.
Journal of microbiological methods, 2024
- Mycobacterium tuberculosis
- Metabolomics
- Metabolome
G. I. Harisa, Saleh A. Alanazi, M. Badran, et al.
European Journal of Lipid Science and Technology, 2023
Md. Akbar, Hasan Ali, Md. Azizur Rahman
Intelligent Pharmacy, 2024
Aim of the study was designed to investigate the antihyperlipidemic activity of carvedilol and pitavastatin in tyloxapol-induced hyperlipidemia in Wistar rats. The rats were randomly divided into 6 groups. The vehicle control group-I received 2 mL of normal saline for eight days. The pathological control group-II received tyloxapol (400 mg/kg) on 8th day. The treated group-III received 10 mg/kg carvedilol and group-IV received 20 mg/kg carvedilol for eight days and tyloxapol (400 mg/kg) on the 8th day. The group-V received pitavastatin (0.3 mg/kg) for eight days and tyloxapol (400 mg/kg) on the 8th day. The group-VI received carvedilol (20 mg/kg) only for eight days. After eight days of treatment, triglycerides, total cholesterol, high-density lipoprotein, very low-density lipoprotein, thiobarbituric acid reactive substances, and glutathione were estimated in the serum and myocardial tissues along with DNA fragmentation of the liver tissue using gel-electrophoresis. Oral administration of carvedilol to tyloxapol-induced hyperlipidemic rats normalized the changes in the above parameters in a dose dependent manner. Hence, carvedilol with pitavastatin has antihyperlipidemic activity in tyloxapol-induced hyperlipidemia in Wistar rats.
Abstract licence: CC BY
Sources: aggregated from Europe PMC (EMBL-EBI), OpenAlex, Crossref, PubMed and other open scholarly databases. Retracted articles are excluded. Study information is provided for research purposes and does not constitute medical advice.
Pharmacology and chemical data from DrugBank
Key facts
Drug status
Approved
Major interactions
None known
Half-life
Not available
Mechanism
Tyloxapol, when injected IP, blocks plasma lipolytic activity, and thus the breakdown of triglyceride-rich lipoproteins.
Food interactions
None known
Human targets
6 targets
Data: DrugBank · CC BY-NC 4.0
Pharmacokinetics at a glance
Proteins and enzymes this drug interacts with in the body
PMID:11342582 PMID:27578112 PMID:8675619
Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity .
PMID:12032167 PMID:7592706
Mediates margination of triglyceride-rich lipoprotein particles in capillaries .
PMID:24726386
Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans PMID:11342582 PMID:27811232
The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors.
NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator
Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family.
In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL.
Stimulates promoter activity in the presence of NFKB2/p49. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a CRY1/CRY2 independent manner.
Increased repression of the heterodimer is seen in the presence of NFKB2/p52. Is required for both T and B lymphocyte maturation and function PMID:26385063
The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. The NF-kappa-B heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function as transcriptional activators.
NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus.
The inhibitory effect of I-kappa-B on NF-kappa-B through retention in the cytoplasm is exerted primarily through the interaction with RELA. RELA shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Besides its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression.
Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells .
PMID:15790681
The NF-kappa-B homodimeric RELA-RELA complex appears to be involved in invasin-mediated activation of IL-8 expression. Key transcription factor regulating the IFN response during SARS-CoV-2 infection PMID:33440148
Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family.
In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator.
The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor.
Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer
ATC R05CA01
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
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Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Linked compound data from DrugBank Open Data (CC BY-NC 4.0)
Tyloxapol
Additional database identifiers
ChemSpider
26330335
HUGO Gene Nomenclature Committee (HGNC)
HGNC:6677
GenAtlas
LPL
GeneCards
LPL
GenBank Gene Database
M15856
GenBank Protein Database
307138
UniProt Accession
LIPL_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9954
GeneCards
REL
UniProt Accession
REL_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9956
GeneCards
RELB
UniProt Accession
RELB_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9955
GeneCards
RELA
Guide to Pharmacology
3280
UniProt Accession
TF65_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:7795
GenAtlas
NFKB2
GeneCards
NFKB2
GenBank Gene Database
X61498
UniProt Accession
NFKB2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:7794
GenAtlas
NFKB1
GeneCards
NFKB1
GenBank Gene Database
M55643
GenBank Protein Database
189180
UniProt Accession
NFKB1_HUMAN
DrugBank citations
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Structured knowledge from the free knowledge base
ATC classifications (Wikidata)
Linked open data from Wikidata (Q7860340), a free and open knowledge base operated by the Wikimedia Foundation. Data is available under the Creative Commons CC0 1.0 Public Domain Dedication.