Premium
DNA topoisomerase I changes the mode of interaction between camptothecin drugs and DNA as probed by UV‐resonance Raman spectroscopy
Author(s) -
Feofanov Alexei V.,
Baranov Alexandre V.,
Fleury Fabrice,
Riou Jean-François,
Nabiev Igor R.,
Manfait Michel
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)01118-0
Subject(s) - resonance raman spectroscopy , camptothecin , dna , raman spectroscopy , topoisomerase , chemistry , spectroscopy , resonance (particle physics) , biophysics , nuclear magnetic resonance , photochemistry , biochemistry , biology , physics , optics , atomic physics , quantum mechanics
Pronounced differences of interactions of camptothecin (CPT) and its derivative 7‐ethyl‐10‐[4‐(1‐piperidino)‐1‐piperidino]carbonyloycamptothecin (CPT11), inhibitors of DNA topoisomerase I, with oligonucleotides were found using UV resonance Raman spectroscopy. 30‐mer oligonucleotides were derived from the sequences of the topoisomerase I‐induced and CPT‐enhanced cleavage sites in SV40 DNA. CPT induces well‐defined alterations of the oligo structure, whereas CPT11 interacts with oligonucleotides more weakly and in another manner than CPT. Formation of cleavable ternary complexes between CPT11, topoisomerase I and oligonucleotides causes CPT11 to interact with oligonucleotides in the same fashion as was found for its parent compound CPT, and enhances this interaction as compared to CPT‐oligonucleotide complexes. The data present evidence of molecular interactions of CPT11 with both other partners (topoisomerase I and oligonucleotide) of the ternary cleavable complex at the oligonucleotide‐enzyme interface.