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- W2000357729 abstract "Distamycin A (Dst) is an antibiotic which binds to the minor groove of double-stranded DNA at A/T-rich regions. We have examined the affinity and mode of Dst binding to DNA duplexes containing a conserved A/T core and variable terminal A/T regions by using circular dichroism spectroscopy. The observed circular dichroism spectra were analyzed by singular value decomposition and fitted to a two-step binding model. The result clearly shows a correlation between the affinity for Dst and the preference for Dst-DNA 1:1 binding over 2:1 binding. The A/T stretches that prefer 1:1 binding form high-affinity 1:1 complexes, whereas those preferring 2:1 binding form stable 2:1 complex with low overall affinities. The terminal A/T residues of the Dst binding region play an important role in the stabilization/destabilization of the 1:1 and 2:1 complexes, resulting in a terminal residue-dependent variation of the binding affinity and the binding mode preference." @default.
- W2000357729 created "2016-06-24" @default.
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- W2000357729 date "2010-06-01" @default.
- W2000357729 modified "2023-10-16" @default.
- W2000357729 title "Binding affinity and mode of distamycin A with A/T stretches in double-stranded DNA: Importance of the terminal A/T residues" @default.
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- W2000357729 doi "https://doi.org/10.1016/j.bpc.2010.03.014" @default.
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