N,N-Bis(2-oxo-3-oxazolidinyl)phosphinic chloride
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N,N-Bis(2-oxo-3-oxazolidinyl)phosphinic chloride

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N,N-Bis(2-oxo-3-oxazolidinyl)phosphinic chloride (CAS# 68641-49-6) is a useful research chemical.

Category
Peptide Synthesis Reagents
Catalog number
BAT-002404
CAS number
68641-49-6
Molecular Formula
C6H8ClN2O5P
Molecular Weight
254.56
N,N-Bis(2-oxo-3-oxazolidinyl)phosphinic chloride
IUPAC Name
3-[chloro-(2-oxo-1,3-oxazolidin-3-yl)phosphoryl]-1,3-oxazolidin-2-one
Synonyms
BOP-Cl; Phosphoric acid bis(2-oxooxazolidide) chloride; BOP-CL; Bis(2-oxo-3-oxazolidinyl)phosphinic chloride; bis(2-oxo-1,3-oxazolidin-3-yl)phosphinic chloride
Appearance
White to off-white crystalline powder
Purity
≥ 98 % (Assay)
Density
1.710±0.10 g/cm3 (Predicted)
Melting Point
191 °C (dec.)
Boiling Point
332.8±25.0 °C (Predicted)
Storage
Store at RT
InChI
InChI=1S/C6H8ClN2O5P/c7-15(12,8-1-3-13-5(8)10)9-2-4-14-6(9)11/h1-4H2
InChI Key
KLDLRDSRCMJKGM-UHFFFAOYSA-N
Canonical SMILES
C1COC(=O)N1P(=O)(N2CCOC2=O)Cl
1. Practical protocols for stepwise solid-phase synthesis of cysteine-containing peptides
Y M Angell, J Alsina, F Albericio, G Barany J Pept Res. 2002 Nov;60(5):292-9. doi: 10.1034/j.1399-3011.2002.02838.x.
This study details a series of conditions that may be applied to ensure 'safe' incorporation of cysteine with minimal racemization during automated or manual solid-phase peptide synthesis. Earlier studies from our laboratories [Han et al. (1997) J. Org. Chem. 62, 4307-4312] showed that several common coupling methods, including those exploiting in situ activating agents such as N-[(dimethylamino)-1H-1,2,3-triazolo[4,5-b]pyridin-1-ylmethylene]-N-methylmethanaminium hexafluorophosphate N-oxide (HATU), N-[1H-benzotriazol-1-yl)-(dimethylamino)methylene]-N-methylmethanaminium hexafluorophosphate N-oxide (HBTU), and (benzotriazol-1-yl-N-oxy)tris(dimethylamino)phosphonium hexafluorophosphate (BOP) [all in the presence of N-methylmorpholine (NMM) or N,N-diisopropylethylamine (DIEA) as a tertiary amine base], give rise to unacceptable levels (i.e. 5-33%) of cysteine racemization. As demonstrated on the tripeptide model H-Gly-Cys-Phe-NH(2), and on the nonapeptide dihydrooxytocin, the following methods are recommended: O-pentafluorophenyl (O-Pfp) ester in DMF; O-Pfp ester/1-hydroxybenzotriazole (HOBt) in DMF; N,N'-diisopropylcarbodiimide (DIPCDI)/HOBt in DMF; HBTU/HOBt/2,4,6-trimethylpyridine (TMP) in DMF (preactivation time 3.5-7.0 min in all of these cases); and HBTU/HOBt/TMP in CH(2)Cl(2)/DMF (1:1) with no preactivation. In fact, several of the aforementioned methods are now used routinely in our laboratory during the automated synthesis of analogs of the 58-residue protein bovine pancreatic trypsin inhibitor (BPTI). In addition, several highly hindered bases such as 2,6-dimethylpyridine (lutidine), 2,3,5,6-tetramethylpyridine (TEMP), octahydroacridine (OHA), and 2,6-di-tert-butyl-4-(dimethylamino)pyridine (DB[DMAP]) may be used in place of the usual DIEA or NMM to minimize cysteine racemization even with the in situ coupling protocols.
2. Lead identification of novel and selective TYK2 inhibitors
Jun Liang, et al. Eur J Med Chem. 2013 Sep;67:175-87. doi: 10.1016/j.ejmech.2013.03.070. Epub 2013 May 14.
A therapeutic rationale is proposed for the treatment of inflammatory diseases, such as psoriasis and inflammatory bowel diseases (IBD), by selective targeting of TYK2. Hit triage, following a high-throughput screen for TYK2 inhibitors, revealed pyridine 1 as a promising starting point for lead identification. Initial expansion of 3 separate regions of the molecule led to eventual identification of cyclopropyl amide 46, a potent lead analog with good kinase selectivity, physicochemical properties, and pharmacokinetic profile. Analysis of the binding modes of the series in TYK2 and JAK2 crystal structures revealed key interactions leading to good TYK2 potency and design options for future optimization of selectivity.
3. Aggrecanase-2 inhibitors based on the acylthiosemicarbazide zinc-binding group
Lucie Maingot, et al. Eur J Med Chem. 2013 Nov;69:244-61. doi: 10.1016/j.ejmech.2013.08.027. Epub 2013 Aug 30.
Osteoarthritis is a disabling disease characterized by the articular cartilage breakdown. Aggrecanases are potential therapeutic targets for the treatment of this pathology. At the starting point of this project, an acylthiosemicarbazide was discovered to inhibit aggrecanase-2. The acylthiosemicarbazide Zn binding group is also a convenient linker for library synthesis. A focused library of 920 analogs was thus prepared and screened to establish structure-activity relationships. The modification of the acylthiosemicarbazide was also explored. This strategy combining library design and discrete compounds synthesis yielded inhibitor 35, that is highly selective for aggrecanases over a panel of metalloproteases and inhibits the degradation of native fully glycosylated aggrecan. A docking study generated binding conformations explaining the structure-activity relationships.
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