Lysozyme is a protein that is present in numerous plant and animal cells, where it provides antimicrobial properties important for immune function. Recent studies have suggested that lysozyme could be utilized for treatment of viral diseases via an interaction with deoxyribonucleic acids (DNA). To investigate the interaction, we used fluorescence spectroscopy and calorimetry to investigate the binding between lysozyme and DNA. Intrinsic Trp fluorescence revealed an intensity decrease upon DNA binding with approximately two nucleotides for each lysozyme molecule. The binding interaction was influenced by ionic strength and the presence of Mg2+ and Ca2+ ions. Such an interaction was further investigated by Differential Scanning Calorimetry, showing the melting temperatures (Tm) for DNA, lysozyme, and the DNA-Lysozyme complex, which were 52, 77, and 95 degrees Celsius, respectively. Isothermal titration calorimetry showed that the association binding constant is in the order of 106 M-1 with a molar enthalpy change of -3.3 kcal/mol. Currently, we are using mutagenesis to probe the possible DNA binding site(s) within lysozyme.

Exploration of the interactions of hen egg white lysozyme with deoxyribonucleic acids

253rd National Meeting (2017)

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