Page last updated: 2024-12-06

2,2'-bisphenol f

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Related Drugs Related Conditions Protein Interactions Research Growth Market Indicators

Description

2,2'-bisphenol F (BPF) is a synthetic organic compound. It is a colorless solid that is used in the production of epoxy resins, polycarbonates, and other polymers. BPF is produced by the condensation reaction of formaldehyde and phenol. It is a persistent organic pollutant that has been detected in the environment and in human tissues. BPF is suspected of being an endocrine disruptor and has been linked to adverse health effects, such as reproductive problems and cancer. BPF is studied because of its potential health risks and its widespread use in industrial products. It is also studied to understand its fate and transport in the environment. '

2,2'-bisphenol F: contact allergen; structure given in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID75575
CHEMBL ID148831
CHEBI ID34207
SCHEMBL ID49745
MeSH IDM0138258

Synonyms (58)

Synonym
BIDD:ER0432
unii-04d0a23747
phenol, 2,2'-methylenedi-
phenol, 2,2'-methylenebis-
nsc 402103
einecs 219-578-2
04d0a23747 ,
2467-02-9
2,2'-methylenebis(phenol)
bis(2-hydroxyphenyl)methane
phenol,2'-methylenedi-
2,2'-dihydroxydiphenylmethane
2,2'-methylenediphenol
o-(o-hydroxybenzyl)phenol
phenol,2'-methylenebis-
nsc402103
nsc-402103
2,2'-bisphenol f
bis(2-hydroxyphenyl)methane, 98%
2-[(2-hydroxyphenyl)methyl]phenol
2-(2-hydroxybenzyl)phenol
CHEMBL148831 ,
chebi:34207 ,
ksc-19-053
KUC106449N
FT-0691346
mqcpolnsjcwpgt-uhfffaoysa-
inchi=1/c13h12o2/c14-12-7-3-1-5-10(12)9-11-6-2-4-8-13(11)15/h1-8,14-15h,9h2
D1939
bis(o-hydroxyphenyl)methane
cas-2467-02-9
tox21_303599
dtxcid602446
dtxsid4022446 ,
NCGC00257306-01
KUC112930N
ksc-336-004-1
methylenebisphenol
1333-16-0
AKOS015912954
SCHEMBL49745
2,2'-bis(hydroxyphenyl)methane
o,o'-bis(hydroxyphenyl)methane
bis-(2-hydroxyphenyl)methane
bis-(hydroxyphenyl)methane
bisphenol-f
bis(hydroxyphenyl) methane
o,o'-methylenediphenol
W-109788
mfcd00002243
AS-58785
2,2'-dihydroxydiphenylmethane, >/=99%
bis-(2-hydroxy-phenyl)-methane
Q27115904
D89951
2,2-bis(hydroxyphenyl)methane
bdbm50522653
2,2-methylenediphenol
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Drug Classes (1)

ClassDescription
diarylmethaneAny compound containing two aryl groups connected by a single C atom.
[compound class information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Protein Targets (13)

Potency Measurements

ProteinTaxonomyMeasurementAverage (µ)Min (ref.)Avg (ref.)Max (ref.)Bioassay(s)
GLI family zinc finger 3Homo sapiens (human)Potency27.48720.000714.592883.7951AID1259369; AID1259392
AR proteinHomo sapiens (human)Potency22.03980.000221.22318,912.5098AID1259243; AID1259247; AID743035; AID743063
estrogen receptor 2 (ER beta)Homo sapiens (human)Potency27.30600.000657.913322,387.1992AID1259378
nuclear receptor subfamily 1, group I, member 3Homo sapiens (human)Potency61.13060.001022.650876.6163AID1224839
progesterone receptorHomo sapiens (human)Potency47.94780.000417.946075.1148AID1346784; AID1346795
pregnane X nuclear receptorHomo sapiens (human)Potency61.13060.005428.02631,258.9301AID1346982
estrogen nuclear receptor alphaHomo sapiens (human)Potency27.53910.000229.305416,493.5996AID743075
peroxisome proliferator activated receptor gammaHomo sapiens (human)Potency30.89940.001019.414170.9645AID743191
v-jun sarcoma virus 17 oncogene homolog (avian)Homo sapiens (human)Potency54.94770.057821.109761.2679AID1159528
thyroid hormone receptor beta isoform 2Rattus norvegicus (Norway rat)Potency64.86010.000323.4451159.6830AID743065; AID743067
nuclear factor erythroid 2-related factor 2 isoform 1Homo sapiens (human)Potency44.51410.000627.21521,122.0200AID743202; AID743219
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Endoplasmic reticulum chaperone BiPHomo sapiens (human)IC50 (µMol)100.00000.80007.02509.1000AID1590351
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Other Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Fatty acid-binding protein, intestinalHomo sapiens (human)K153.00000.50000.50000.5000AID71603
Fatty acid-binding protein, intestinalHomo sapiens (human)K230.00000.40000.40000.4000AID71604
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (29)

Processvia Protein(s)Taxonomy
ER overload responseEndoplasmic reticulum chaperone BiPHomo sapiens (human)
cerebellum structural organizationEndoplasmic reticulum chaperone BiPHomo sapiens (human)
cerebellar Purkinje cell layer developmentEndoplasmic reticulum chaperone BiPHomo sapiens (human)
substantia nigra developmentEndoplasmic reticulum chaperone BiPHomo sapiens (human)
positive regulation of cell migrationEndoplasmic reticulum chaperone BiPHomo sapiens (human)
negative regulation of transforming growth factor beta receptor signaling pathwayEndoplasmic reticulum chaperone BiPHomo sapiens (human)
endoplasmic reticulum unfolded protein responseEndoplasmic reticulum chaperone BiPHomo sapiens (human)
post-translational protein targeting to membrane, translocationEndoplasmic reticulum chaperone BiPHomo sapiens (human)
negative regulation of protein-containing complex assemblyEndoplasmic reticulum chaperone BiPHomo sapiens (human)
positive regulation of protein ubiquitinationEndoplasmic reticulum chaperone BiPHomo sapiens (human)
protein folding in endoplasmic reticulumEndoplasmic reticulum chaperone BiPHomo sapiens (human)
response to endoplasmic reticulum stressEndoplasmic reticulum chaperone BiPHomo sapiens (human)
maintenance of protein localization in endoplasmic reticulumEndoplasmic reticulum chaperone BiPHomo sapiens (human)
ERAD pathwayEndoplasmic reticulum chaperone BiPHomo sapiens (human)
cellular response to glucose starvationEndoplasmic reticulum chaperone BiPHomo sapiens (human)
negative regulation of apoptotic processEndoplasmic reticulum chaperone BiPHomo sapiens (human)
positive regulation of transcription by RNA polymerase IIEndoplasmic reticulum chaperone BiPHomo sapiens (human)
regulation of protein folding in endoplasmic reticulumEndoplasmic reticulum chaperone BiPHomo sapiens (human)
cellular response to interleukin-4Endoplasmic reticulum chaperone BiPHomo sapiens (human)
regulation of ATF6-mediated unfolded protein responseEndoplasmic reticulum chaperone BiPHomo sapiens (human)
regulation of IRE1-mediated unfolded protein responseEndoplasmic reticulum chaperone BiPHomo sapiens (human)
negative regulation of IRE1-mediated unfolded protein responseEndoplasmic reticulum chaperone BiPHomo sapiens (human)
regulation of PERK-mediated unfolded protein responseEndoplasmic reticulum chaperone BiPHomo sapiens (human)
chaperone cofactor-dependent protein refoldingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
protein refoldingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
fatty acid metabolic processFatty acid-binding protein, intestinalHomo sapiens (human)
long-chain fatty acid transportFatty acid-binding protein, intestinalHomo sapiens (human)
intestinal lipid absorptionFatty acid-binding protein, intestinalHomo sapiens (human)
fatty acid transportFatty acid-binding protein, intestinalHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (18)

Processvia Protein(s)Taxonomy
calcium ion bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
protein bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
ATP bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
ATP hydrolysis activityEndoplasmic reticulum chaperone BiPHomo sapiens (human)
enzyme bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
protein domain specific bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
ubiquitin protein ligase bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
ribosome bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
cadherin bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
unfolded protein bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
protein-folding chaperone bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
misfolded protein bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
ATP-dependent protein folding chaperoneEndoplasmic reticulum chaperone BiPHomo sapiens (human)
protein folding chaperoneEndoplasmic reticulum chaperone BiPHomo sapiens (human)
heat shock protein bindingEndoplasmic reticulum chaperone BiPHomo sapiens (human)
long-chain fatty acid transmembrane transporter activityFatty acid-binding protein, intestinalHomo sapiens (human)
fatty acid bindingFatty acid-binding protein, intestinalHomo sapiens (human)
protein bindingFatty acid-binding protein, intestinalHomo sapiens (human)
long-chain fatty acid bindingFatty acid-binding protein, intestinalHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (21)

Processvia Protein(s)Taxonomy
COP9 signalosomeEndoplasmic reticulum chaperone BiPHomo sapiens (human)
nucleusEndoplasmic reticulum chaperone BiPHomo sapiens (human)
cytoplasmEndoplasmic reticulum chaperone BiPHomo sapiens (human)
mitochondrionEndoplasmic reticulum chaperone BiPHomo sapiens (human)
endoplasmic reticulumEndoplasmic reticulum chaperone BiPHomo sapiens (human)
endoplasmic reticulum lumenEndoplasmic reticulum chaperone BiPHomo sapiens (human)
endoplasmic reticulum membraneEndoplasmic reticulum chaperone BiPHomo sapiens (human)
endoplasmic reticulum-Golgi intermediate compartmentEndoplasmic reticulum chaperone BiPHomo sapiens (human)
cytosolEndoplasmic reticulum chaperone BiPHomo sapiens (human)
plasma membraneEndoplasmic reticulum chaperone BiPHomo sapiens (human)
focal adhesionEndoplasmic reticulum chaperone BiPHomo sapiens (human)
cell surfaceEndoplasmic reticulum chaperone BiPHomo sapiens (human)
membraneEndoplasmic reticulum chaperone BiPHomo sapiens (human)
midbodyEndoplasmic reticulum chaperone BiPHomo sapiens (human)
melanosomeEndoplasmic reticulum chaperone BiPHomo sapiens (human)
intracellular membrane-bounded organelleEndoplasmic reticulum chaperone BiPHomo sapiens (human)
extracellular exosomeEndoplasmic reticulum chaperone BiPHomo sapiens (human)
protein-containing complexEndoplasmic reticulum chaperone BiPHomo sapiens (human)
endoplasmic reticulum chaperone complexEndoplasmic reticulum chaperone BiPHomo sapiens (human)
endoplasmic reticulum lumenEndoplasmic reticulum chaperone BiPHomo sapiens (human)
cytoplasmEndoplasmic reticulum chaperone BiPHomo sapiens (human)
nucleusEndoplasmic reticulum chaperone BiPHomo sapiens (human)
membraneEndoplasmic reticulum chaperone BiPHomo sapiens (human)
cytosolFatty acid-binding protein, intestinalHomo sapiens (human)
microvillusFatty acid-binding protein, intestinalHomo sapiens (human)
apical cortexFatty acid-binding protein, intestinalHomo sapiens (human)
cytosolFatty acid-binding protein, intestinalHomo sapiens (human)
nucleusFatty acid-binding protein, intestinalHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (6)

Assay IDTitleYearJournalArticle
AID71604In vitro inhibitory activity against wild-type intestinal Fatty acid-binding protein (FabI) of Escherichia coli expressed as K22004Journal of medicinal chemistry, Jan-29, Volume: 47, Issue:3
Inhibition of the bacterial enoyl reductase FabI by triclosan: a structure-reactivity analysis of FabI inhibition by triclosan analogues.
AID1590351Inhibition of GRP78 (26 to 636 residues) (unknown origin) expressed in Escherichia coli BL21 DE3 cells pre-incubated for 10 mins before FITC-NRLLLTG fluorescent peptide addition in presence of 20 uM ADP followed by further incubation for 2 hrs by fluoresc2019Bioorganic & medicinal chemistry letters, 07-15, Volume: 29, Issue:14
A high throughput substrate binding assay reveals hexachlorophene as an inhibitor of the ER-resident HSP70 chaperone GRP78.
AID1254100Binding affinity to human PRDX5 expressed in Escherichia coli by STD NMR spectrometric analysis2015Journal of medicinal chemistry, Nov-12, Volume: 58, Issue:21
Ligand-Orientation Based Fragment Selection in STD NMR Screening.
AID69489Minimum inhibitory concentration against Escherichia coli was determined2004Journal of medicinal chemistry, Jan-29, Volume: 47, Issue:3
Inhibition of the bacterial enoyl reductase FabI by triclosan: a structure-reactivity analysis of FabI inhibition by triclosan analogues.
AID71603In vitro inhibitory activity against wild-type intestinal Fatty acid-binding protein (FabI) of Escherichia coli expressed as K12004Journal of medicinal chemistry, Jan-29, Volume: 47, Issue:3
Inhibition of the bacterial enoyl reductase FabI by triclosan: a structure-reactivity analysis of FabI inhibition by triclosan analogues.
AID71606Ionisation constant for the compoound; ND means Not determined2004Journal of medicinal chemistry, Jan-29, Volume: 47, Issue:3
Inhibition of the bacterial enoyl reductase FabI by triclosan: a structure-reactivity analysis of FabI inhibition by triclosan analogues.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (8)

TimeframeStudies, This Drug (%)All Drugs %
pre-19902 (25.00)18.7374
1990's1 (12.50)18.2507
2000's3 (37.50)29.6817
2010's2 (25.00)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 12.47

According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be weak demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index12.47 (24.57)
Research Supply Index2.20 (2.92)
Research Growth Index4.66 (4.65)
Search Engine Demand Index0.00 (26.88)
Search Engine Supply Index0.00 (0.95)

This Compound (12.47)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies1 (12.50%)4.05%
Observational0 (0.00%)0.25%
Other7 (87.50%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]