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Merck
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文件

SML2328

Sigma-Aldrich

BD064

≥98% (HPLC)

别名:

B-[5-[[[1-[3-(4-Ethoxyphenyl)-3,4-dihydro-4-oxopyrido[2,3-d]pyrimidin-2-yl]ethyl][2-[4-fluoro-3-(trifluoromethyl)phenyl]acetyl]amino]methyl]-2-fluorophenyl]boronic acid

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About This Item

经验公式（希尔记法）:
C33H28BF5N4O5
CAS号:
1630085-92-5
分子量:
666.40
分類程式碼代碼:
12352200
NACRES:
NA.77

化驗

≥98% (HPLC)

形狀

powder

儲存條件

desiccated

顏色

white to beige

溶解度

DMSO: 2 mg/mL, clear

儲存溫度

−20°C

SMILES 字串

O=C1N(C2=CC=C(OCC)C=C2)C(C(N(C(CC3=CC=C(F)C(C(F)(F)F)=C3)=O)CC4=CC(B(O)O)=C(F)C=C4)C)=NC5=NC=CC=C51

生化／生理作用

BD064 is a probe-dependent and biased negative allosteric modulator (NAM) of the chemokine receptor CXCR3 signaling that preferentially inhibits CXCL11-mediated ?-arrestin 2 recruitment over G protein activation.

儲存類別代碼

11 - Combustible Solids

水污染物質分類（WGK）

WGK 3

閃點（°F）

Not applicable

閃點（°C）

Not applicable

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Viachaslau Bernat et al.
ChemMedChem, 10(3), 566-574 (2015-02-07)
Over the last decade, functional selectivity (or ligand bias) has evolved from being a peculiar phenomenon to being recognized as an essential feature of synthetic ligands that target G protein-coupled receptors (GPCRs). The CXC chemokine receptor 3 (CXCR3) is an outstanding platform
Regine Brox et al.
Molecular pharmacology, 93(4), 309-322 (2018-01-19)
Our recent explorations of allosteric modulators with improved properties resulted in the identification of two biased negative allosteric modulators, BD103 (N-1-{[3-(4-ethoxyphenyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimi-din2yl]ethyl}-4-(4-fluorobutoxy)-N-[(1-methylpiperidin-4-yl)methyl}]butanamide) and BD064 (5-[(N-{1-[3-(4-ethoxyphenyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-2-yl]ethyl-2-[4-fluoro-3-(trifluoromethyl)phenyl]acetamido)methyl]-2-fluorophenyl}boronic acid), that exhibited probe-dependent inhibition of CXC-motif chemokine receptor CXCR3 signaling. With the intention to elucidate
Viachaslau Bernat et al.
ACS chemical biology, 9(11), 2664-2677 (2014-09-19)
The chemokine receptor CXCR3 is a G protein-coupled receptor, which conveys extracellular signals into cells by changing its conformation upon agonist binding. To facilitate the mechanistic understanding of allosteric modulation of CXCR3, we combined computational modeling with the synthesis of

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