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Drug-Target Interaction

Drug

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PubChem ID:445154
Structure:
Synonyms:
"trans-3,4′,5-trihydroxystilbene"
(E)-5-(2-(4-hydroxyphenyl)ethenyl)-1,3-benzenediol
(E)-5-(p-Hydroxystyryl)resorcinol
(E)-5-[2-(4-hydroxyphenyl)ethenyl]-1,3-benzendiol
(E)-5-[2-(4-Hydroxyphenyl)ethenyl]-1,3-benzenediol
(E)-resveratrol
1,3-Benzenediol, 5-(2-(4-hydroxyphenyl)ethenyl)-, (E)-
1,3-Benzenediol, 5-(2-(4-hydroxyphenyl)ethenyl)-, (E)-;
3,4',5-Stilbenetriol
3,4',5-trihydroxy-stilbene
3,4',5-Trihydroxy-trans-stilbene
3,4',5-Trihydroxystilbene
3,5,4'-Trihydroxy-trans-stilbene
3,5,4'-Trihydroxystilbene
3,5-Dihydroxy-4'-methoxystilbene
31100-06-8
31100-06-8 (DELETED)
34092_FLUKA
34092_RIEDEL
5-((1E)-2-(4-Hydroxyphenyl)ethenyl)-1,3-benzenediol
5-[(1E)-2-(4-Hydroxyphenyl)ethenyl]-1,3-benzenediol
5-[(1E)-2-(4-hydroxyphenyl)ethenyl]benzene-1,3-diol
5-[(1E)-2-(4-hydroxyphenyl)vinyl]benzene-1,3-diol
5-[(E)-2-(4-hydroxyphenyl)ethenyl]benzene-1,3-diol
5-[(E)-2-(4-hydroxyphenyl)vinyl]benzene-1,3-diol
5-[2-(4-hydroxyphenyl)ethenyl]benzene-1,3-diol
501-36-0
533C1DA0-4104-42B5-9D32-9265F40857E4
AC-727
AC1L9HIC
AIDS-025474
AIDS025474
BB_NC-2570
BPBio1_000479
BRD-K25591257-001-01-2
BRD-K80738081-001-06-2
BRD-K80738081-001-10-4
BSPBio_000435
BSPBio_001114
BSPBio_003461
C03582
C059514
C14H12O3
CCG-38874
CCRIS 8952
CHEBI:27881
CHEBI:45713
CHEMBL165
CPD-83
CPD000058206
CU-01000001503-3
DB02709
EU-0101111
FT-0082623
HMS1362H15
HMS1569F17
HMS1792H15
HMS1921N04
HMS1990H15
HMS2052I09
HMS2096F17
HMS2232A18
HMS3263O04
HSDB 7571
I06-0437
IDI1_002152
KSC-10-164
KUC104385N
LMPK13090005
Lopac0_001111
LS-2146
LUKBXSAWLPMMSZ-OWOJBTEDSA-
MLS000069735
MLS001055357
MLS001076538
MLS002207121
MLS002222231
MolPort-002-499-801
NCGC00017352-05
NCGC00017352-06
NCGC00017352-07
NCGC00017352-08
NCGC00017352-09
NCGC00017352-10
NCGC00017352-11
NCGC00017352-12
NCGC00017352-13
NCGC00017352-14
NCGC00017352-15
NCGC00017352-16
NCGC00017352-17
NCGC00017352-18
NCGC00017352-19
NCGC00024003-00
NCGC00024003-04
NCGC00024003-05
NCGC00024003-06
NCGC00024003-07
NCGC00024003-08
NCGC00024003-09
NCGC00024003-10
NCGC00024003-11
NCGC00024003-12
NCGC00024003-13
NCGC00024003-14
nchembio.140-comp2
nchembio.281-comp10
NSC 327430
NSC327430
Prestwick2_000508
Prestwick3_000508
Prestwick_619
PREVENTION 8 (RESVERATROL)
R 5010
R0071
R5010_SIGMA
Resveratrol
Resveratrol, E-
resveratrol-3-sulfate
Resveratrol-Supplied by Selleck Chemicals
Resvida
RM-1812
RV
S1396_Selleck
SAM001246888
SDCCGMLS-0002998.P003
SGCUT00007
SMR000058206
SPECTRUM1502223
Spectrum5_000552
SRT 501
SRT-501
SRT501
ST057251
STL
TL8003323
to_000079
trans-1,2-(3,4',5-Trihydroxydiphenyl)ethylene
trans-3,4′,5-Trihydroxystilbene
trans-3,4',5-trihydroxystilbene
trans-Resveratrol
ZINC00006787

Target

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Uniprot ID:CP1A1_HUMAN
Synonyms:
CYPIA1
Cytochrome P450 1A1
P450 form 6
P450-C
P450-P1
EC-Numbers:1.14.14.1
Organism:Homo sapiens
Human
PDB IDs:-

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----
----
----

References:

10496959
Inhibition of aryl hydrocarbon-induced cytochrome P-450 1A1 enzyme activity and CYP1A1 expression by resveratrol.. H P Ciolino; G C Yeh (1999) Molecular pharmacology display abstract
We investigated the effect of resveratrol, a constituent of the human diet that has been shown to inhibit aryl hydrocarbon-induced carcinogenesis in animals, on the carcinogen activation pathway regulated by the aryl hydrocarbon receptor. Resveratrol inhibited the metabolism of the environmental aryl hydrocarbon benzo[a]pyrene (B[a]P) catalyzed by microsomes isolated from B[a]P-treated human hepatoma HepG2 cells. Resveratrol competitively inhibited, in a concentration-dependent manner, the activity of the carcinogen activating enzymes cytochrome P-450 (CYP)1A1/CYP1A2 in microsomes and intact HepG2 cells. Resveratrol inhibited the B[a]P-induced expression of the CYP1A1 gene, as measured at the mRNA and transcriptional levels. Resveratrol abolished the binding of B[a]P-activated nuclear aryl hydrocarbon receptor to the xenobiotic-responsive element of the CYP1A1 promoter but did not itself bind to the receptor. Resveratrol was also effective in inhibiting CYP1A1 transcription induced by the aryl hydrocarbon dimethylbenz[a]anthracene in human mammary carcinoma MCF-7 cells. These data demonstrate that resveratrol inhibits aryl hydrocarbon-induced CYP1A activity in vitro by directly inhibiting CYP1A1/1A2 enzyme activity and by inhibiting the signal transduction pathway that up-regulates the expression of carcinogen activating enzymes. These activities may be an important part of the chemopreventive activity of resveratrol in vivo.
11714871
Differential inhibition and inactivation of human CYP1 enzymes by trans-resveratrol: evidence for mechanism-based inactivation of CYP1A2.. T K Chang; J Chen; W B Lee (2001) The Journal of pharmacology and experimental therapeutics display abstract
trans-Resveratrol (3,5,4'-trihydroxy-trans-stilbene) has been reported to confer chemoprotection against 7,12-dimethylbenz[a]anthracene (DMBA)-induced carcinogenicity in a murine model. A potential mechanism for this effect by trans-resveratrol is inhibition of DMBA-bioactivating cytochrome P450 (CYP) enzymes such as CYP1B1, CYP1A1, and CYP1A2. In the present study, we examined in detail the in vitro inhibitory effects of trans-resveratrol on these three human CYP enzymes. trans-Resveratrol decreased 7-ethoxyresorufin O-dealkylation activity catalyzed by human recombinant CYP1B1, CYP1A1, and CYP1A2 in a concentration-dependent manner and by a mixed type of inhibition. This direct inhibition was enzyme-selective, as judged by the differences in the apparent K(i) values (0.8 +/- 0.1 microM, 1.2 +/- 0.1 microM, and 15.5 +/- 1.1 microM for CYP1B1, CYP1A1, and CYP1A2, respectively). Preincubating recombinant CYP1A2 or human liver microsomes with trans-resveratrol and NADPH prior to the initiation of substrate oxidation resulted in a time- and concentration-dependent decrease in catalytic activity. The inactivation of liver microsomal CYP1A2 by trans-resveratrol required NADPH, was not reversible by dialysis, and was not affected by the trapping agents glutathione, N-acetylcysteine, catalase, or superoxide dismutase, but was attenuated by a CYP1A2 substrate, imipramine. Analysis of a panel of individual human liver microsomes showed intersample differences in the response to the in vitro inactivation by trans-resveratrol. In contrast to CYP1A2, CYP1B1 was not subject to inactivation by this compound and the reduction in CYP1A1 activity was time- but not concentration-dependent. In summary, trans-resveratrol differentially inhibited human CYP1 enzymes and this occurred by two distinct mechanisms: direct inhibition (mainly CYP1B1 and CYP1A1) and mechanism-based inactivation (CYP1A2).
17440990
Inhibition of human recombinant cytochromes P450 CYP1A1 and CYP1B1 by trans-resveratrol methyl ethers.. Renata Mikstacka; Dorota Przybylska; Agnes M Rimando; Wanda Baer-Dubowska (2007) Molecular nutrition & food research display abstract
CYP1A1 and CYP1B1 are the inducible forms of cytochrome P450 expressed in extrahepatic tissues, which are responsible for the biotransformation of polycyclic aromatic hydrocarbons, heterocyclic amines and estradiol to the carcinogenic intermediates. The aim of our research was to determine and compare the inhibitory effect of naturally occurring analogues of trans-resveratrol on the catalytic activities of human recombinant CYP1A1 and CYP1B1. Pinostilbene (3,4'-dihydroxy-5-methoxystilbene), desoxyrhapontigenin (3,5-dihydroxy-4'-methoxystilbene), and pterostilbene (3,5-dimethoxy-4'-hydroxystilbene) appeared to be very potent inhibitors of CYP1A1 catalytic activity with Ki values of 0.13, 0.16 and 0.57 microM, respectively. Results from this study indicate that trans-resveratrol analogues in which the hydroxy groups are substituted by methoxy groups exhibit a remarkably stronger inhibitory effect towards CYP1A1 in comparison to the parent compound. On the contrary, the potency of pinostilbene, desoxyrhapontigenin and pterostilbene towards CYP1B1 with Ki values of 0.90, 2.06 and 0.91 microM, respectively, was comparable to that of resveratrol. It appears that between these analogues, inhibition of CYP1A1 and CYP1B1 catalytic activities does not vary much regardless of the number and position of methylether substitution. The results suggest that the trans-resveratrol analogues: pinostilbene, desoxyrhapontigenin and pterostilbene, which occur in some food plants, might be considered as promising chemopreventive agents.