Specific interaction between a novel enediyne chromophore and apoprotein in macromolecular antitumor antibiotic C-1027.
The DNA cleavage experiments show that C-1027 chromophore is selectively incorporated into C-1027 apoprotein and is strongly protected by the apoprotein from loss of its DNA cleaving activity. Fluorescence and circular dichroism spectra reveal (1) important participation of tertiary structure of C-1027 apoprotein for the chromophore binding, (2) specific 1:1 binding of C-1027 chromophore to the apoprotein, and (3) significant interaction of the benzoxazine group in the chromophore-apoprotein complex. On the other hand, C-1027 apoprotein does not contribute to sequence-specificity DNA cleavage by C-1027 antibiotics.
Institute for Chemical Research, Kyoto University, Japan.
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T
Matsumoto
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Okuno
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Y
Sugiura
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D000903:Antibiotics, Antineoplastic / Q000737:chemistry*; D001059:Apoproteins / Q000737:chemistry*; D002942:Circular Dichroism; D004247:DNA / Q000032:analysis; D053281:Enediynes; D008961:Models, Structural; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D013050:Spectrometry, Fluorescence
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D000903:Antibiotics, Antineoplastic; D001059:Apoproteins; D053281:Enediynes; D011506:Proteins; C058024:C 1027; D004247:DNA