Specific enzyme-induced decapsulation
Little difficulty exists in finding chemotherapeutic agents that kill pathological cells; the problem lies in identifying agents that do so without damaging normal cells as well. One possible route to selectivity plays on the fact that certain pathological cells produce excessive amounts of a partic...
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Published in | Journal of the American Chemical Society Vol. 113; no. 14; pp. 5467 - 5468 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
01.07.1991
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Subjects | |
Online Access | Get full text |
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Summary: | Little difficulty exists in finding chemotherapeutic agents that kill pathological cells; the problem lies in identifying agents that do so without damaging normal cells as well. One possible route to selectivity plays on the fact that certain pathological cells produce excessive amounts of a particular enzyme (e.g., bone cancer/alkaline phosphatase, neuroblastoma/acetylcholinesterase). If such an enzyme is capable of breaking open specially designed vesicles that encapsulate a cytotoxic drug, then selective therapeutic activity toward the enzyme-exuding cell can be achieved. We describe herein compound I which, in concert with acetylcholinesterase (AcE), models the above process. |
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Bibliography: | istex:EAF305516A14CDEEF12CF4C6E504CDB166C02C48 ark:/67375/TPS-X2B7M1ZJ-9 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0002-7863 1520-5126 |
DOI: | 10.1021/ja00014a056 |