Document Detail


Synthesis and biological evaluation of poly-gamma-glutamyl metabolites of 10-deazaaminopterin and 10-ethyl-10-deazaaminopterin.
MedLine Citation:
PMID:  2447278     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The chemical synthesis of a series of poly-gamma-glutamyl metabolites of the experimental anticancer drugs 10-deazaaminopterin (10-DAAM) and 10-ethyl-10-deazaaminopterin (10-EDAAM) has been carried out by the solid-phase procedure. The synthetic products were identical with the poly-gamma-glutamyl metabolites of radiolabeled 10-DAAM and 10-EDAAM produced by normal mouse tissues with regard to elution volume from [(diethylamino)ethyl]cellulose columns and susceptibility to hydrolysis by human plasma folylpolyglutamate hydrolase. Poly-gamma-glutamyl metabolites with a glutamate chain length of up to four glutamate residues were detected in the tissues. The antifolate activity was evaluated with methotrexate (MTX) sensitive and MTX-resistant strains of Lactobacillus casei and Streptococcus faecium. In general, inhibitory potency decreases with increasing Glu chain length. However there are two exceptions. Addition of one Glu residue to 10-DAAM enhances its potency for MTX-resistant L. casei and addition of one Glu residue to 10-EDAAM enhances its potency for the MTX-sensitive L. casei. As shown earlier for MTX polyglutamates, polyglutamylation greatly enhances the inhibitory potency of 10-DAAM and 10-EDAAM for L. casei thymidylate synthase. MTX polyglutamates are 15-30 times more inhibitory than the corresponding 10-DAAM derivatives and 30-60 times more inhibitory than the corresponding 10-EDAAM derivatives. Polyglutamylation of 10-DAAM had little influence on its ability to inhibit L. casei dihydrofolate reductase; however, with 10-EDAAM, addition of one or two Glu residues enhanced its inhibitory potency 2.3-fold.
Authors:
M G Nair; N T Nanavati; P Kumar; Y Gaumont; R L Kisliuk
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of medicinal chemistry     Volume:  31     ISSN:  0022-2623     ISO Abbreviation:  J. Med. Chem.     Publication Date:  1988 Jan 
Date Detail:
Created Date:  1988-02-17     Completed Date:  1988-02-17     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9716531     Medline TA:  J Med Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  181-5     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of South Alabama, Mobile 36688.
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MeSH Terms
Descriptor/Qualifier:
Aminopterin / analogs & derivatives*,  pharmacology
Animals
Anti-Bacterial Agents / chemical synthesis*
Female
Folic Acid Antagonists / pharmacology*
Humans
Lactobacillus casei / drug effects
Methotrexate / pharmacology
Mice
Mice, Inbred Strains
Microbial Sensitivity Tests
Peptides / chemical synthesis*
Polyglutamic Acid / analogs & derivatives,  chemical synthesis*,  pharmacology
Streptococcus / drug effects
Structure-Activity Relationship
Substrate Specificity
gamma-Glutamyl Hydrolase / blood
Grant Support
ID/Acronym/Agency:
CA 10914/CA/NCI NIH HHS; CA 27101/CA/NCI NIH HHS; CA 32687/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/Folic Acid Antagonists; 0/Peptides; 25513-46-6/Polyglutamic Acid; 52454-37-2/10-deazaaminopterin; 54-62-6/Aminopterin; 59-05-2/Methotrexate; 80576-83-6/edatrexate; EC 3.4.19.9/gamma-Glutamyl Hydrolase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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