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Reference

Synthesis and structure-activity relations of bestatin analogs, inhibitors of aminopeptidase B
Synthesis and structure-activity relations of bestatin analogs, inhibitors of aminopeptidase B. Nishizawa, Rinzo; Saino, Tetsushi; Takita, Tomohisa; Suda, Hiroyuki; Aoyagi, Takaaki; Umezawa, Hamao (Pharm. Div.In this study, 62023-59-0 and 62023-27-2 are also used., Nippon Kayaku Co., Ltd., Tokyo, Japan). J. Med. Chem., 20(4), 510-15 (English) 1977. CODEN: JMCMAR. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacodynamics) Section cross-reference(s): 7, 34 Stereoisomers and analogs of bestatin [[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]-L-leucine] [58970-76-6] were synthesized and tested for aminopeptidase B [9073-92-1] and leucine aminopeptidase [9001-61-0] inhibiting activity. Among the 8 stereoisomers, the 2S stereoisomers exhibited strong activity. In a series of compds. in which the L-leucine residue of bestatin was substituted with other amino acids, only the one contg. isoleucine [62023-75-0] showed more activity than bestatin. Norleucine [62023-76-1], norvaline [62023-74-9], methionine [62023-72-7], valine [62023-73-8], serine [62023-71-6], glutamine [62023-70-5], phenylalanine [62023-77-2], glutamic acid [62023-69-2], proline [62023-67-0], and lysine [62023-68-1] analogs gave, in that order, decreasing activity. Alkyl and phenyl substitution for the benzyl group of bestatin decreased the activity markedly. P-methyl- [62023-80-7], p-chloro- [62023-79-4], and p-nitrobestatin [62023-78-3] showed greater activity than bestatin. .
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