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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.
J Med Chem ; 18(8): 826-30, 1975 Aug.
Article in En | MEDLINE | ID: mdl-1159700
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.
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Collection: 01-internacional Database: MEDLINE Main subject: Amantadine / Dipeptides / Leucyl Aminopeptidase Limits: Animals Language: En Journal: J Med Chem Journal subject: QUIMICA Year: 1975 Type: Article
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Collection: 01-internacional Database: MEDLINE Main subject: Amantadine / Dipeptides / Leucyl Aminopeptidase Limits: Animals Language: En Journal: J Med Chem Journal subject: QUIMICA Year: 1975 Type: Article