SML2782
Br-PBTC
≥98% (HPLC)
别名:
(R)-7-Bromo-N-(piperidin-3-yl)benzo[b]thiophene-2-carboxamide, 7-Bromo-N-(3R)-3-piperidinylbenzo[b]thiophene-2-carboxamide
质量水平
方案
≥98% (HPLC)
表单
powder
颜色
white to beige
溶解性
DMSO: 2 mg/mL, clear
储存温度
2-8°C
SMILES字符串
O=C(C1=CC(C=CC=C2Br)=C2S1)N[C@@H]3CCCNC3
InChI
1S/C14H15BrN2OS/c15-11-5-1-3-9-7-12(19-13(9)11)14(18)17-10-4-2-6-16-8-10/h1,3,5,7,10,16H,2,4,6,8H2,(H,17,18)/t10-/m1/s1
InChI key
LRYYPTVUWGMZQB-SNVBAGLBSA-N
生化/生理作用
Br-PBTC is a selective and potent type II positive allosteric modulator (PAM) that potentiates the opening of the nicotinic acetylcholine receptors (nAChR) subtypes containing α4β2, α2β2 and α2β4 subunits. Br-PBTC potentiates opening and reactivates desensitized (α4β2)2α4 nAChRs. It appears that Br-PBTC interacts with extracellular C-terminus of α2 or α4 in association with nearby parts of the α subunit.
selective and potent type II PAM that potentiates the opening of the nAChR subtypes containing α4β2, α2β2 and α2β4 subunits.
储存分类代码
11 - Combustible Solids
WGK
WGK 3
法规信息
新产品
此项目有
Jingyi Wang et al.
The Journal of biological chemistry, 290(48), 28834-28846 (2015-10-04)
Positive allosteric modulators (PAMs) of nicotinic acetylcholine receptors (nAChR) are important therapeutic candidates as well as valuable research tools. We identified a novel type II PAM, (R)-7-bromo-N-(piperidin-3-yl)benzo[b]thiophene-2-carboxamide (Br-PBTC), which both increases activation and reactivates desensitized nAChRs. This compound increases acetylcholine-evoked
Jack Norleans et al.
The Journal of biological chemistry, 294(32), 12132-12145 (2019-06-22)
Nicotinic acetylcholine receptor (nAChR) ligands that lack agonist activity but enhance activation in the presence of an agonist are called positive allosteric modulators (PAMs). nAChR PAMs have therapeutic potential for the treatment of nicotine addiction and several neuropsychiatric disorders. PAMs
Jingyi Wang et al.
British journal of pharmacology, 175(11), 1805-1821 (2017-02-16)
Heteromeric nicotinic ACh receptors (nAChRs) were thought to have two orthodox agonist-binding sites at two α/β subunit interfaces. Highly selective ligands are hard to develop by targeting orthodox agonist sites because of high sequence similarity of this binding pocket among
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