42361-78-4Relevant academic research and scientific papers
Synthesis and hypotensive activities of octahydropyrazinopyridoindoles and 15-azayohimbanes
Valls, N.,Segarra, V. M.,Tost, A.,Rosell, G.
, p. 899 - 902 (2007/10/02)
The hypotensive activities in rats of indolic compounds 1-9 were compared with that of reserpine.In spite of differences in their structure, all 9 showed similar hypotensive activities to that of reserpine.New octahydropyrazinopyridoindoles 3-6 and the te
Angiotensin-converting enzyme inhibitors: Synthesis and biological activity of acyl tripeptide analogues of enalapril
Greenlee,Allibone,Perlow,Patchett,Ulm,Vassil
, p. 434 - 442 (2007/10/02)
The synthesis and biological activity of a series of inhibitors of angiotensin-converting enzyme (EC 3.4.15.1) are described. Incorporation of the substituted N-carboxymethyl dipeptide design of enalapril (MK-421) into acyl tripeptides and larger peptides
Thiohemiacetal formation by inhibitory aldehydes at the active site of papain.
Lewis,Wolfenden
, p. 4890,4891 (2007/10/05)
Papain is strongly inhibited by aldehydes resembling carboxylic acids, released by hydrolysis of specific substrates (Westerik, J. O''C., and Wolfenden, R. (1972), J. Biol. Chem. 247, 8195-8197). Inhibitory complexes might involve binding of the aldehyde intact or as a covalent hydrate, or the aldehyde might undergo covalent addition of an active site sulfhydryl group to form a thiohemiacetal derivative. In an attempt to distinguish between these possibilities, benzamidoacetaldehyde-1-d has been synthesized, and its properties compared with those of the undeuterated inhibitor. After correction for differences in hydration, the observed effect on inhibition is found to be compatible with formation of a thiohemiacetal. In keeping with this conclusion, benzamidoethanol (a partial analogue of the covalent hydrate) and benzamide, N-methylbenzamide and N-ethylbenzamide (somewhat similar to the free aldehyde in size and hydrophobic character) are found to exhibit negligible affinity for the active site.
