SML1770
PhiKan083 hydrochloride
≥98% (HPLC)
Synonyme(s) :
9-Ethyl-N-methyl-9H-Carbazole-3-methanamine hydrochloride, PK-083 hydrochloride, PK083 hydrochloride, PhiKan-083 hydrochloride
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A propos de cet article
Formule empirique (notation de Hill) :
C16H18N2 · HCl
Numéro CAS:
Poids moléculaire :
274.79
UNSPSC Code:
12352200
NACRES:
NA.77
MDL number:
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assay
≥98% (HPLC)
form
powder
storage condition
desiccated
color
white to beige
solubility
H2O: 2 mg/mL, clear
storage temp.
2-8°C
SMILES string
CNCC1=CC2=C(C=C1)N(CC)C3=C2C=CC=C3.[H]Cl
InChI key
IXWVUPURFWFRNE-UHFFFAOYSA-N
Biochem/physiol Actions
Mutant p53 stabilizer
PhiKan083 is a small molecule that binds within a cavity on the surface of Y220C-mutated p53. This mutation, which is not involved in DNA interaction, causes a destabilization of the protein. PhiKan083 binding acts to stabilize the mutant p53 and slow the rate of denaturation.
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Matthias R Bauer et al.
ACS chemical biology, 11(8), 2265-2274 (2016-06-09)
Many oncogenic mutants of the tumor suppressor p53 are conformationally unstable, including the frequently occurring Y220C mutant. We have previously developed several small-molecule stabilizers of this mutant. One of these molecules, PhiKan083, 1-(9-ethyl-9H-carbazole-3-yl)-N-methylmethanamine, binds to a mutation-induced surface crevice with
Joana Soares et al.
Oncotarget, 7(4), 4326-4343 (2016-01-07)
Restoration of the p53 pathway, namely by reactivation of mutant (mut) p53, represents a valuable anticancer strategy. Herein, we report the identification of the enantiopure tryptophanol-derived oxazoloisoindolinone SLMP53-1 as a novel reactivator of wild-type (wt) and mut p53, using a
Frank M Boeckler et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(30), 10360-10365 (2008-07-25)
The tumor suppressor p53 is mutationally inactivated in approximately 50% of human cancers. Approximately one-third of the mutations lower the melting temperature of the protein, leading to its rapid denaturation. Small molecules that bind to those mutants and stabilize them