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Biochimie. 2013 Sep;95(9):1689-96. doi: 10.1016/j.biochi.2013.04.013. Epub 2013 May 7.

Physicochemical characterization of the staphylolytic LysK enzyme in complexes with polycationic polymers as a potent antimicrobial.

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Department of Chemical Enzymology, Faculty of Chemistry, M.V. Lomonosov Moscow State University, Vorobievy Gory, 1-11, Moscow 119991, Russia.


Staphylococcus aureus causes many serious visceral, skin, and respiratory diseases. About 90% of its clinical strains are multi-drug resistant, but the use of bacteriophage lytic enzymes offers a viable alternative to antibiotic therapy. LysK, the phage K endolysin, can lyse S. aureus when purified and exposed externally. It has been investigated in its complexes with polycationic polymers (poly-l-lysines (PLLs) of molecular weights 2.5, 9.6, and 55.2 kDa and their block copolymers with polyethylene glycol PLL10-PEG114, PLL30-PEG114, and PLL30-PEG23) as a basis for creating active and stable antimicrobial. Complexing with polycationic PLLs produces a stabilizing effect on LysK due to structure ordering in its molecules and break-down of aggregates as a result of electrostatic interaction. The stability of LysK in the presence of PLL-PEG block copolymers improves by both electrostatic and hydrophobic mechanisms. Complexes of LysK with 2.5, 9.6, 55.2 kDa poly-l-lysines and PLL30-PEG114 have demonstrated sufficient stability at the temperatures of physiological activity (37 °C) and storage (4 °C and 22 °C).


A(600); Antibacterial enzymes; DLS; FTIR; Fourier-transform infrared spectroscopy; LMW; MRSA; PLL; PLL(x)–PEG(y); Polycation; Stability; Stabilization; Staphylococcal infections; dynamic light scattering; half-inactivation time; low molecular weight; methicillin-resistant Staphylococcus aureus; optical density at 600 nm; poly-l-lysine hydrobromide; poly-l-lysine hydrobromide–polyethylene glycol block copolymer, x and y values correspond to a number of l-lysine and ethylene glycol structural units; τ(1/2)

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