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L. Y. Filatova, D. M. Donovan, J. A. Foster-Frey, V. G. Pugachev, E. V. Kudryashova, N. L. Klyachko
Lytic
enzymes of staphylococcal phages: correlation between secondary structure and
stability
Abstract
Lytic enzymes of bacteriophages K, phi11 and phi80α are able to lyse (destroy) cells
of antibiotic resistant strains of Staphylococcus aureus, and they can
be considered as promising antimicrobial agents. The stability of recombinant
lysins of phages K, phi11 and phi80α was investigated in conditions of storage and functioning,
and the relationship between the stability and the secondary structure of the
enzymes was found. It was shown that the lower the content of disordered
structures in the molecules of enzymes, the greater the stability of lysins
(half-inactivation time). Beta-structural lysin of phage phi11 shows the best
stability at storage temperature (22°C), both lysin of phage K with
alpha-helical structure and lysin of phage phi80α with disordered secondary structure are less stable.
Key words: Staphylococcus aureus, phage lysins,
secondary structure, stability
Copyright (C) Chemistry Dept., Moscow State University, 2002
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