Physicochemical characterization of the staphylolytic LysK enzyme in complexes with polycationic polymers as a potent antimicrobial.
Biochimie
; 95(9): 1689-96, 2013 Sep.
Article
em En
| MEDLINE
| ID: mdl-23665361
ABSTRACT
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).
Palavras-chave
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 hydrobromidepolyethylene glycol block copolymer, x and y values correspond to a number of l-lysine and ethylene glycol structural units; τ(1/2)
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Polímeros
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Staphylococcus aureus
/
Fenômenos Químicos
Idioma:
En
Revista:
Biochimie
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Federação Russa