Page last updated: 2024-11-06

phenylethane boronic acid

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

Phenylethane boronic acid is an organoboron compound with the formula C6H5CH2B(OH)2. It is a colorless solid that is used as a building block in organic synthesis. It is particularly useful in Suzuki-Miyaura couplings, a palladium-catalyzed cross-coupling reaction that is widely used to form carbon-carbon bonds. This reaction allows for the construction of complex molecules, including pharmaceuticals and natural products. Phenylethane boronic acid is commercially available and can be synthesized via a variety of methods, including the reaction of phenylmagnesium bromide with trimethyl borate, followed by hydrolysis. This compound is of significant interest in the field of medicinal chemistry due to its potential to be incorporated into a wide range of drug candidates. Its ability to form new carbon-carbon bonds with a variety of partners opens up new avenues for the development of novel therapeutics.'

Cross-References

ID SourceID
PubMed CID65389
CHEMBL ID20461
SCHEMBL ID129543
MeSH IDM0112839

Synonyms (36)

Synonym
AC-5344
bdbm26142
(2-phenylethyl)boranediol
2-phenylethylboronic acid
phenylethane boronic acid
phenethylboronic acid ,
DB01963
34420-17-2
CHEMBL20461
2-phenylethyl boronic acid
AKOS005254522
NCGC00249462-01
boronic acid, (2-phenylethyl)-
peba
FT-0639191
AB09361
VPRUMANMDWQMNF-UHFFFAOYSA-N
phenethyl boronic acid
SCHEMBL129543
2-phenyl-1-ethylboronic acid
SY014651
mfcd01631226
phenethylboronicacid
(2-phenylethyl)boronic acid
2-phenylethaneboronic acid
J-510243
DTXSID10188000
CS-W000915
PS-9619
2-phenylethane boronic acid
Q27093058
P2476
2-phenylethylboronic acid (contains varying amounts of anhydride)
AMY13278
EN300-91342
Z1147227790
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (5)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Carbonic anhydrase 1Homo sapiens (human)Ki11.40000.00001.372610.0000AID424442
Carbonic anhydrase 2Homo sapiens (human)Ki17.90000.00000.72369.9200AID424443
Fatty-acid amide hydrolase 1Rattus norvegicus (Norway rat)IC50 (µMol)1.30000.00051.33138.0000AID1798637; AID346655
Carbonic anhydraseCandida albicans SC5314Ki412.00000.01051.44448.3470AID424445
Monoglyceride lipaseHomo sapiens (human)IC50 (µMol)1.30000.00091.126810.0000AID1798637
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (23)

Processvia Protein(s)Taxonomy
one-carbon metabolic processCarbonic anhydrase 1Homo sapiens (human)
morphogenesis of an epitheliumCarbonic anhydrase 2Homo sapiens (human)
positive regulation of synaptic transmission, GABAergicCarbonic anhydrase 2Homo sapiens (human)
positive regulation of cellular pH reductionCarbonic anhydrase 2Homo sapiens (human)
angiotensin-activated signaling pathwayCarbonic anhydrase 2Homo sapiens (human)
regulation of monoatomic anion transportCarbonic anhydrase 2Homo sapiens (human)
secretionCarbonic anhydrase 2Homo sapiens (human)
regulation of intracellular pHCarbonic anhydrase 2Homo sapiens (human)
neuron cellular homeostasisCarbonic anhydrase 2Homo sapiens (human)
positive regulation of dipeptide transmembrane transportCarbonic anhydrase 2Homo sapiens (human)
regulation of chloride transportCarbonic anhydrase 2Homo sapiens (human)
carbon dioxide transportCarbonic anhydrase 2Homo sapiens (human)
one-carbon metabolic processCarbonic anhydrase 2Homo sapiens (human)
lipid metabolic processMonoglyceride lipaseHomo sapiens (human)
fatty acid biosynthetic processMonoglyceride lipaseHomo sapiens (human)
inflammatory responseMonoglyceride lipaseHomo sapiens (human)
regulation of signal transductionMonoglyceride lipaseHomo sapiens (human)
arachidonic acid metabolic processMonoglyceride lipaseHomo sapiens (human)
triglyceride catabolic processMonoglyceride lipaseHomo sapiens (human)
acylglycerol catabolic processMonoglyceride lipaseHomo sapiens (human)
regulation of inflammatory responseMonoglyceride lipaseHomo sapiens (human)
regulation of sensory perception of painMonoglyceride lipaseHomo sapiens (human)
monoacylglycerol catabolic processMonoglyceride lipaseHomo sapiens (human)
regulation of endocannabinoid signaling pathwayMonoglyceride lipaseHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (9)

Processvia Protein(s)Taxonomy
arylesterase activityCarbonic anhydrase 1Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 1Homo sapiens (human)
protein bindingCarbonic anhydrase 1Homo sapiens (human)
zinc ion bindingCarbonic anhydrase 1Homo sapiens (human)
hydro-lyase activityCarbonic anhydrase 1Homo sapiens (human)
cyanamide hydratase activityCarbonic anhydrase 1Homo sapiens (human)
arylesterase activityCarbonic anhydrase 2Homo sapiens (human)
carbonate dehydratase activityCarbonic anhydrase 2Homo sapiens (human)
protein bindingCarbonic anhydrase 2Homo sapiens (human)
zinc ion bindingCarbonic anhydrase 2Homo sapiens (human)
cyanamide hydratase activityCarbonic anhydrase 2Homo sapiens (human)
lysophospholipase activityMonoglyceride lipaseHomo sapiens (human)
protein bindingMonoglyceride lipaseHomo sapiens (human)
protein homodimerization activityMonoglyceride lipaseHomo sapiens (human)
acylglycerol lipase activityMonoglyceride lipaseHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (8)

Processvia Protein(s)Taxonomy
cytosolCarbonic anhydrase 1Homo sapiens (human)
extracellular exosomeCarbonic anhydrase 1Homo sapiens (human)
cytoplasmCarbonic anhydrase 2Homo sapiens (human)
cytosolCarbonic anhydrase 2Homo sapiens (human)
plasma membraneCarbonic anhydrase 2Homo sapiens (human)
myelin sheathCarbonic anhydrase 2Homo sapiens (human)
apical part of cellCarbonic anhydrase 2Homo sapiens (human)
extracellular exosomeCarbonic anhydrase 2Homo sapiens (human)
cytoplasmCarbonic anhydrase 2Homo sapiens (human)
plasma membraneCarbonic anhydrase 2Homo sapiens (human)
apical part of cellCarbonic anhydrase 2Homo sapiens (human)
endoplasmic reticulum membraneMonoglyceride lipaseHomo sapiens (human)
cytosolMonoglyceride lipaseHomo sapiens (human)
plasma membraneMonoglyceride lipaseHomo sapiens (human)
membraneMonoglyceride lipaseHomo sapiens (human)
membraneMonoglyceride lipaseHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (10)

Assay IDTitleYearJournalArticle
AID437828Inhibition of penicillin-resistant Streptococcus pneumoniae 5204 PBP2X assessed as residual activity at 1000 uM preincubated for 4 hrs before addition of substrate mixture of (R)-[2-(benzoylamino)propionylsulfanyl]acetic acid and 5,5'-dithiobis(2-nitroben2009Journal of medicinal chemistry, Oct-08, Volume: 52, Issue:19
Synthesis and evaluation of 3-(dihydroxyboryl)benzoic acids as D,D-carboxypeptidase R39 inhibitors.
AID437817Inhibition of Actinomadura sp. R39 penicillin-binding protein assessed as residual activity at 1000 uM preincubated for 60 mins before addition of substrate mixture of (R)-[2-(benzoylamino)propionylsulfanyl]acetic acid and 5,5'-dithiobis(2-nitrobenzoic ac2009Journal of medicinal chemistry, Oct-08, Volume: 52, Issue:19
Synthesis and evaluation of 3-(dihydroxyboryl)benzoic acids as D,D-carboxypeptidase R39 inhibitors.
AID346655Inhibition of Wistar rat brain FAAH assessed as [3H]arachidonoylethanolamide hydrolysis2008Journal of medicinal chemistry, Nov-27, Volume: 51, Issue:22
Discovery of boronic acids as novel and potent inhibitors of fatty acid amide hydrolase.
AID346657Inhibition of human recombinant MGL at 100 uM2008Journal of medicinal chemistry, Nov-27, Volume: 51, Issue:22
Discovery of boronic acids as novel and potent inhibitors of fatty acid amide hydrolase.
AID424444Inhibition of Cryptococcus neoformans recombinant Carbonic anhydrase 2 pre-incubated for 15 mins by CO2 hydration stopped-flow assay2009Bioorganic & medicinal chemistry letters, May-15, Volume: 19, Issue:10
Carbonic anhydrase inhibitors. Inhibition of the fungal beta-carbonic anhydrases from Candida albicans and Cryptococcus neoformans with boronic acids.
AID437825Inhibition of penicillin-sensitive Streptococcus pneumoniae R6 PBP2X assessed as residual activity at 1000 uM preincubated for 60 mins before addition of substrate mixture of (R)-[2-(benzoylamino)propionylsulfanyl]acetic acid and 5,5'-dithiobis(2-nitroben2009Journal of medicinal chemistry, Oct-08, Volume: 52, Issue:19
Synthesis and evaluation of 3-(dihydroxyboryl)benzoic acids as D,D-carboxypeptidase R39 inhibitors.
AID424445Inhibition of Candida albicans recombinant Carbonic anhydrase pre-incubated for 15 mins by CO2 hydration stopped-flow assay2009Bioorganic & medicinal chemistry letters, May-15, Volume: 19, Issue:10
Carbonic anhydrase inhibitors. Inhibition of the fungal beta-carbonic anhydrases from Candida albicans and Cryptococcus neoformans with boronic acids.
AID424443Inhibition of human recombinant cytosolic carbonic anhydrase 2 preincubated for 15 mins by CO2 hydration stopped-flow assay2009Bioorganic & medicinal chemistry letters, May-15, Volume: 19, Issue:10
Carbonic anhydrase inhibitors. Inhibition of the fungal beta-carbonic anhydrases from Candida albicans and Cryptococcus neoformans with boronic acids.
AID424442Inhibition of human recombinant cytosolic carbonic anhydrase 1 preincubated for 15 mins by CO2 hydration stopped-flow assay2009Bioorganic & medicinal chemistry letters, May-15, Volume: 19, Issue:10
Carbonic anhydrase inhibitors. Inhibition of the fungal beta-carbonic anhydrases from Candida albicans and Cryptococcus neoformans with boronic acids.
AID1798637FAAH Inhibition Assay from Article 10.1021/jm801051t: \\Discovery of Boronic Acids as Novel and Potent Inhibitors of Fatty Acid Amide Hydrolase.\\2008Journal of medicinal chemistry, Nov-27, Volume: 51, Issue:22
Discovery of boronic acids as novel and potent inhibitors of fatty acid amide hydrolase.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (12)

TimeframeStudies, This Drug (%)All Drugs %
pre-19903 (25.00)18.7374
1990's0 (0.00)18.2507
2000's3 (25.00)29.6817
2010's2 (16.67)24.3611
2020's4 (33.33)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 12.30

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 Index12.30 (24.57)
Research Supply Index2.56 (2.92)
Research Growth Index4.86 (4.65)
Search Engine Demand Index0.00 (26.88)
Search Engine Supply Index0.00 (0.95)

This Compound (12.30)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other12 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]