126111-17-9Relevant academic research and scientific papers
Conformational studies on peptides of α-aminoxy acids with functionalized side-chains
Yang, Dan,Liu, Guo-Jun,Hao, Yu,Li, Wei,Dong, Ze-Min,Zhang, Dan-Wei,Zhu, Nian-Yong
, p. 1356 - 1363 (2010)
Peptides of homochiral α- aminoxy acids of nonpolar side chains can form a 1.88-helix. In this paper, we report the conformational studies of α- aminoxy peptides 1-3, which have functionalized side chains, in both non- polar and polar solvents.
(Phosphinyloxy)acid amino acid inhibitors of angiotensin converting enzyme. 2. Terminal amino acid analogues of (S)-1-[6-Amino-2-[[hydroxy(4-phenylbutyl)phosphinyl]oxy]-1-oxohexyl]- L-proline
Karanewsky,Badia,Cushman,DeForrest,Dejneka,Lee,Loots,Petrillo
, p. 1459 - 1469 (2007/10/02)
Analogues of (S)-1-[6-amino-2-[[hydroxy(4-phenylbutyl)phosphinyl]oxy]-1-oxohexyl]- L-proline (1, SQ 29,852) in which the terminal proline residue has been replaced by a variety of substituted and heteroatom-substituted prolines, N-arylglycines, N-cycloalkylglycines, and bicyclic amino acids have been synthesized and evaluated as inhibitors of angiotensin converting enzyme in vitro an in vivo. In general, the addition of lipophilic substituents to the 4-position of proline of the parent phosphate 1 resulted in substantial increases in vitro activity. The largest improvements were observed in the case of cis-benzyl (36-fold) and dithioketal (24-fold) analogues 2r and 2x, respectively. These enhancements of in vitro activity were accompanied by modest increases (2-3.5-fold) in in vivo (iv) activity. Among the various terminal amino acid replacements examined in this study, the indoline-based analogue 2i was by far the most potent compound on iv administration in the normotensive rat.
