14295-48-8Relevant articles and documents
Palladium Catalyzed Hydrogenation of α,β-Unsaturated Sulfones and Phosphonates
Cho, In Sik,Alper, Howard
, p. 4027 - 4028 (1994)
The binuclear palladium complex, 2, when treated with oxygen, catalyzes the hydrogenation of the double bond of α,β-unsaturated sulfones and phosphonates in THF at room temperature and 1 atm of hydrogen pressure.Saturated sulfones and phosphonates were isolated in 49-93percent yields.
N(α)-(diphenoxyphosphoryl)-L-alanyl-L-proline, N(α)-[bis(4-nitrophenoxy)phosphoryl]-L-alanyl-L-proline, and N(α)-[2-phenylethyl)phenoxyphosphoryl]-L-alanyl-L-proline: Releasers of potent inhibitors of angiotensin converting enzyme at physiological pH and temperature
Galardy,Grobelny
, p. 1422 - 1427 (2007/10/02)
The rate of loss of phenol or 4-nitrophenol from N(α)-(diphenoxyphosphoryl)-L-proline (2), N(α)-[bis(4-nitrophenoxy)phosphoryl]-L-alanyl-L-proline (5), and N(α)-[(2-phenylethyl-phenoxyphosphoryl]-L-analyl-L-proline (12) was determined spectrophotometrically at pH 7.5 and 37° C in both Tris and phosphate buffers. These moderately potent inhibitors of angiotensin converting enzyme (K(i) > 0.8 μM) all hydrolyze, losing 1 mol of phenol to yield highly potent inhibitors (K(i) = 0.5-18 nM). The half-times for loss of 1 mol of phenol in Tris buffer are 22 days (2), 3.4 h (5), and 21 days (12). The half-times in phosphate buffer were not significantly different. The mono(4-nitrophenoxy) ester (K(i) = 18 nM) loses its 1 mol of nitrophenol with a half-time of 35 h to yield N(α)-phosphoryl-L-alanyl-L-proline (K(i) = 1.4 nM), which hydrolyzes at the P-N bond with a half-time of 2.2 h. Hydrolysis of the P-N bond in 2 and 12 was not observed during the time course of the kinetic experiments. The two phosphoramidate diesters 2 and 5 and the phosphonamidate monoester 12 thus release powerful inhibitors of angiotensin converting enzyme with a known time course at physiological pH and temperature in vitro. A time-dependent increase in inhibitory potency against converting enzyme that paralleled the kinetics of phenyl ester hydrolysis was confirmed in vitro.
