Inactivating-Effect of Bifunctional Lysine Derivatives on Phage J 1

Abstract

The synthesis and phage-inactivating activity of a homologous series of bifunctional lysine derivatives were previously reported. Here we report on the possible mechanism of phage-inactivating action of the derivatives, using tridecanedioyl-lysine ethyl ester and phage J1 as a model system. In several experiments, azelaoyl-, heptadecanedioyl- and eicosanedioyl-lysine ethyl esters were also used. The addition of chelating agents, neutral amino acids, ribose, deoxyribose, bases, and nucleosides had little effect on the inactivation of phage by the derivatives. Metal cations, basic or acidic amino acids, and nucleotides inhibited the inactivation. In addition, binding of the derivatives was observed to DNA isolated from the phage. The results indicate that the interaction of ε-amino groups of the derivatives with the phosphate residues of phage DNA could be primarily responsible for the inactivation of phage. No differences were demonstrated in phage particles before and after inactivation by CsCl density gradient sedimentation or electron microscopy. © 1984, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.