Kinetics of in vitro hydrolysis of homocamptothecins as measured by fluorescence

Annals of the New York Academy of Sciences

Volumn 922, Issue , 2000, Pages 314-316

  Chauvier, D ^a   Chourpa, I ^b   Bigg, D C H ^a   Manfait, M ^a,c  

^a UNIVERSITÉ DE REIMS CHAMPAGNE ARDENNE   (France)

^b Laboratoire de Chimie Physique   (France)

^c Institut Henri Beaufour   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CAMPTOTHECIN DERIVATIVE; DNA TOPOISOMERASE; HOMOCAMPTOTHECIN DERIVATIVE; LACTONE; UNCLASSIFIED DRUG;

ANTINEOPLASTIC ACTIVITY; CANCER; CONFERENCE PAPER; DNA CLEAVAGE; DRUG HYDROLYSIS; FLUORESCENCE; IN VITRO STUDY; KINETICS; PH;

EID: 0034509642     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2000.tb07052.x     Document Type: Conference Paper

References (6)

1. Homocamptothecin, an E-ring modified camptothecin with enhanced lactone stability, retains topoisomerase I-targeted activity and antitumour properties
2. Effect of local DNA sequence on topoisomerase I cleavage in the presence or absence of camptothecin
3. Kinetics of lactone hydolysis in antitumour drugs of camptothecin series as studied by fluorescence spectroscopy
4. Topotecan lactone selectivity binds to double and single-stranded DNA in the absence of topoisomerase I
5. Modulation of kinetics of lactone ring hydrolysis of camptothecins upon interaction with topoisomerase I cleavage sites on DNA
6. DNA interactions of two clinical camptothecin drugs stabilize their active lactone forms