(dA.dT)-dependent inactivation of the DNA template properties by interaction with netropsin and distamycin A

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Abstract
The inhibitory effect of the polypeptide antibiotics netropsin and distauycin A on DNA dependent nucleic acid synthesis has been shown to be related to the base composition of the template DNA. A number of natural DRA's of quite different dA.dT content as well as poly (dl-dC).poly (dl-dC), poly (dA–dT). poly (dA-dT), poly (dA) . poly (dT) and poly (dG).poly(dC) has been studied as templates in DNA and in part in RNA polymerase reaction, The highest binding efficiency of netropsin existing for (dA.dT)-containins DNA polymers and the less pronounced interaction with the (dI.dC)-containing polymer shown by the melting and CD spectral behaviour of the complexes are entirely reflected in the template inactivation. The same is evident for distamycin A. However, in contrast to netropsin the antibiotic distamycin A exhibits some binding tendency to poly (dG).poly (dC). Binding effects of a netropsin derivative to DNA and (dA.dT)-containing polymers suggest the importance of hydrogen bonds of the peptide groups in the complex for mation.