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Potential latentiation forms of biologically active compounds based on action of leucine aminopeptidase. Dipeptide derivatives of the tricycloaliphatic alpha-amino acid, adamantanine.

Abstract：

:Some glycine, leucine and phenylalanine dipeptide derivatives of the transport inhibitory, tricycloaliphatic alpha-amino acid, adamantanine (1), have been synthesized using classical methods of peptide synthesis with the aim of improving the latter's bioavailability. Although test doses of glycyladamantanine and L-leucyladamantanine appeared to be absorbed in vivo as evidenced by its appearance in the uring following intraperitoneal administration, they were not hydrolyzed by a purified preparation of leucine aminopeptidase in vitro. Indeed, they were inhibitors of this enzyme. Adamantanylglycine, adamantanyl-L-leucine, and adamantanyl-L-phenylalanine were also not hydrolyzed by leucine aminopeptidase.

journal_name

J Med Chem

journal_title

Journal of medicinal chemistry

authors

Nagasawa HT,Elberling JA,Shirota FN

doi

10.1021/jm00242a013

keywords:

subject

Has Abstract

pub_date

1975-08-01 00:00:00

pages

826-30

issue

8

eissn

0022-2623

issn

1520-4804

journal_volume

18

pub_type

杂志文章

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