Resorcinol 50% in Glycerol
Requires a prescription from a doctor or prescriber
Resorcinol is a 1,3-isomer (or meta-isomer) of benzenediol with the formula C6H4(OH)2.
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Suspected adverse reactions reported for Resorcinol
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Suspected adverse reactions reported for Resorcinol
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1 branded products available
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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Codes for healthcare professionals and prescribing systems
These codes are used by healthcare IT systems and prescribers to identify this medicine.
NHS UK identifiers
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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 29 studies.
Reviews & meta-analyses: 2 · 1957–2026
Showing all 29 studies, sorted by most relevant.
Sattwick Haldar, Debanjan Chakraborty, Bibhisan Roy, et al.
Journal of the American Chemical Society, 2018
Yuan Chen, Xiaoying Liu, Si Zhang, et al.
Electrochimica Acta, 2017
L. Svennerholm
Biochimica et biophysica acta, 1957
G. Veselov, A. Vedyagin
Materials, 2023
Carbon xerogels (CXs) are materials obtained via the pyrolysis of resins prepared via the sol-gel polycondensation of resorcinol and formaldehyde. These materials attract great attention as adsorbents, catalyst supports, and energy storage materials. One of the most interesting features of CXs is the possibility of fine-tuning their structures and textures by changing the synthesis conditions in the sol-gel stage. Thus, the first part of this review is devoted to the processes taking place in the polycondensation stage of organic precursors. The formation of hydroxymethyl derivatives of resorcinol and their polycondensation take place at this stage. Both of these processes are catalyzed by acids or bases. It is revealed that the sol-gel synthesis conditions, such as pH, the formaldehyde/resorcinol ratio, concentration, and the type of basic modifier, all affect the texture of the materials being prepared. The variation in these parameters allows one to obtain CXs with pore sizes ranging from 2-3 nm to 100-200 nm. The possibility of using other precursors for the preparation of organic aerogels is examined as well. For instance, if phenol is used instead of resorcinol, the capabilities of the sol-gel method become rather limited. At the same time, other phenolic compounds can be applied with great efficiency. The methods of gel drying and the pyrolysis conditions are also reviewed. Another important aspect analyzed within this review is the surface modification of CXs by introducing various functional groups and heteroatoms. It is shown that compounds containing nitrogen, sulfur, boron, or phosphorus can be introduced at the polycondensation stage to incorporate these elements into the gel structure. Thus, the highest surface amount of nitrogen (6-11 at%) was achieved in the case of the polycondensation of formaldehyde with melamine and hydroxyaniline. Finally, the methods of preparing metal-doped CXs are overviewed. Special attention is paid to the introduction of a metal precursor in the gelation step. The elements of the iron subgroup (Fe, Ni, Co) were found to catalyze carbon graphitization. Therefore, their introduction can be useful for enhancing the electrochemical properties of CXs. However, since the metal surface is often covered by carbon, such materials are poorly applicable to conventional catalytic processes. In summary, the applications of CXs and metal-doped CXs are briefly mentioned. Among the promising application areas, Li-ion batteries, supercapacitors, fuel cells, and adsorbents are of special interest.
Abstract licence: CC BY
T. Iftikhar, M. Asif, A. Aziz, et al.
Trends in Environmental Analytical Chemistry, 2021
Aman Dubey, Ashutosh Kumar Singh, Asha Sharma, et al.
Applied Physics A, 2023
M. Mirzaeian, Qaisar Abbas, D. Gibson, et al.
Energy, 2019
Khalil Ahmad, K. Naseem, H. Shah, et al.
Zeitschrift für Physikalische Chemie, 2023
Morane Beaumet, L. M. Lazinski, Marc Maresca, et al.
Chemmedchem, 2024
- Enzyme Inhibitors
- Melanins
- Resorcinols
Tyrosinases (TYRs) are copper-containing metalloenzymes present in a large diversity of species. In human, hTYR is responsible for pivotal steps in melanogenesis, catalysing the oxidation of l-tyrosine to l-DOPA and further to dopaquinone. While numerous TYR inhibitors have been reported, polyphenolic compounds tend to dominate the literature. However, many of these compounds, particularly monophenols and catechols, have been identified as alternative substrates rather than true inhibitors, given their structural similarity to natural substrates. Resorcinol-containing compounds have emerged as promising candidates to address this challenge, as the meta-dihydroxy moiety in resorcinol demonstrates resistance to TYR-mediated oxidation, while retaining the favourable interactions with copper ions provided by the hydroxy groups. Although their precise mechanism of action remains debated, resorcinol derivatives have yielded some of the most active compounds against isolated mushroom and human TYRs, as well as clinically used dermocosmetic agents like rucinol and thiamidol, which exhibited very promising effects in patients with facial melasma. This review outlines the development of resorcinol-containing TYR inhibitors, categorized by scaffold type, ranging from simple alkyl analogues to intricate synthetic derivatives. Mechanistic insights about the resorcinol-TYR interaction are also presented and debated.
Abstract licence: CC BY
Qingyin Zhang, Xianmei Deng, M. Ji, et al.
Ionics, 2020
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
14 hours
Mechanism
Data regarding the specific mechanisms of action of resorcinol does not appear t…
Food interactions
None known
Human targets
5 targets
Data: DrugBank · CC BY-NC 4.0
Pharmacokinetics at a glance
Absorption
1%
[L2744]
Half-life
90%
Protein binding
Volume of distribution
Metabolism
[L2744]…
Elimination
[L2744]…
Clearance
Pharmacokinetic data: DrugBank · CC BY-NC 4.0
Although it is primarily indicated for use as a topical application, resorcinol also possesses a well-documented anti-thyroidal activity that is generally not relied upon for any kind of formal therapeutic indication.
Known interactions with other medications. Always consult a healthcare professional.
Showing 50 of 753 interactions
It is believed that the Fe3+ of the porphyrin residue of the peroxidase to is oxidised to Fe4+ by hydrogen peroxide with the transfer of an oxygen radical [F61, L2747]. In LPO and TPO, the resulting π-cation radical of the porphyrin can isomerize to a radical cation with the radical in an aromatic side chain of the enzyme [F61, L2747]. The latter radical can bind, in a pH-dependent reaction, covalently and irreversibly to the resorcinol radical formed during regular oxidation of resorcinol and this reduces the activity of the enzyme greatly [F61, L2747]. While the inactivation of the enzyme and the binding of resorcinol to the enzyme may be largely increased by the presence of 0.1 nM iodide, increasing the iodide concentration to 5 mM reduced the resorcinol binding to the enzyme by one quarter but increased the enzyme activity, determined as the rate of iodination of tyrosine, more than proportionally from 6.2% to 44.7% [F61, L2747]. Nevertheless, the role played by iodide ions in the irreversible inactivation of the enzymes is not yet fully elucidated [F61, L2747].
Ultimately, such in vitro and in vivo data propose that the anti-thyroidal activity of resorcinol is caused by inhibition of thyroid peroxidase enzymes, resulting in decreased thyroid hormone production and increased proliferation due to an increase in the secretion of TSH (thyroid stimulating hormone) [F61, L2747]. The iodination process is catalyzed by a haem-containing enzyme, and resorcinol is known to form covalent bonds with haem [F61, L2747].
Despite the legitimacy of this pharmacodynamic profile in resorcinol, the therapeutic uses for which it may be formally indicated for at this time do not actually rely upon any of these mechanisms or dynamics, which are primarily elicited only upon systemic exposure to resorcinol or particularly high overdosage of the agent. This is especially true, considering resorcinol is most commonly available as topical applications to the public.
How the body processes this drug — absorption, distribution, metabolism, and elimination
[L2744]
[L2744]
[L2744]
[L2744]
[L2744]
Proteins and enzymes this drug interacts with in the body
The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons .
PMID:7947975
Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells (Probable).
Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity)
PMID:11327835 PMID:11802772 PMID:11831900 PMID:12056894 PMID:12171926 PMID:1336460 PMID:14736236 PMID:15300855 PMID:15453828 PMID:15667203 PMID:15865431 PMID:16106378 PMID:16214338 PMID:16290146 PMID:16686544 PMID:16759856 PMID:16807956 PMID:17127057 PMID:17251017 PMID:17314045 PMID:17330962 PMID:17346964 PMID:17540563 PMID:17588751 PMID:17705204 PMID:18024029 PMID:18162396 PMID:18266323 PMID:18374572 PMID:18481843 PMID:18618712 PMID:18640037 PMID:18942852 PMID:1909891 PMID:1910042 PMID:19170619 PMID:19186056 PMID:19206230 PMID:19520834 PMID:19778001 PMID:7761440 PMID:7901850 PMID:8218160 PMID:8262987 PMID:8399159 PMID:8451242 PMID:8485129 PMID:8639494 PMID:9265618 PMID:9398308
Can also hydrate cyanamide to urea .
PMID:10550681 PMID:11015219
Stimulates the chloride-bicarbonate exchange activity of SLC26A6 .
PMID:15990874
Essential for bone resorption and osteoclast differentiation .
PMID:15300855
Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption
ATC D10AX02
ATC S01AX06
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)
Resorcinol
Additional database identifiers
Drugs Product Database (DPD)
8689
ChemSpider
4878
BindingDB
26189
PDB
RCO
ZINC
ZINC000000002028
HUGO Gene Nomenclature Committee (HGNC)
HGNC:12015
GenAtlas
TPO
GeneCards
TPO
GenBank Gene Database
J02969
GenBank Protein Database
339867
Guide to Pharmacology
2526
UniProt Accession
PERT_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9604
GenAtlas
PTGS1
GeneCards
PTGS1
GenBank Gene Database
M31822
GenBank Protein Database
387018
Guide to Pharmacology
1375
UniProt Accession
PGH1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:1372
GeneCards
CA14
GenBank Gene Database
AB025904
GenBank Protein Database
6009640
Guide to Pharmacology
2598
UniProt Accession
CAH14_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:1373
GenAtlas
CA2
GeneCards
CA2
GenBank Gene Database
M77181
GenBank Protein Database
179780
Guide to Pharmacology
3092
UniProt Accession
CAH2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:1371
GenAtlas
CA12
GeneCards
CA12
GenBank Gene Database
AF051882
GenBank Protein Database
2984693
Guide to Pharmacology
2747
UniProt Accession
CAH12_HUMAN
DrugBank citations
If you use DrugBank data in your research, please cite the following publications:
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Structured knowledge from the free knowledge base
Linked open data from Wikidata (Q408865), a free and open knowledge base operated by the Wikimedia Foundation. Data is available under the Creative Commons CC0 1.0 Public Domain Dedication.