Complex coacervate core micelles with a lysozyme-modified corona

This paper describes the preparation, characterization, and enzymatic activity of complex coacervate core micelles (C3Ms) composed of poly(acrylic acid) (PAA) and poly(N-methyl-2-vinyl pyridinium iodide)-b-poly(ethylene oxide) (PQ2VP-PEO) to which the antibacterial enzyme lysozyme is end-attached. C...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 23(2007), 15 vom: 17. Juli, Seite 8003-9
1. Verfasser: Danial, Maarten (VerfasserIn)
Weitere Verfasser: Klok, Harm-Anton, Norde, Willem, Stuart, Martien A Cohen
Format: Aufsatz
Sprache:English
Veröffentlicht: 2007
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Comparative Study Journal Article Research Support, Non-U.S. Gov't Acrylic Resins Enzymes, Immobilized Micelles Vinyl Compounds poly(N-methyl-2-vinyl pyridinium iodide)-b-poly(ethylene oxide) Polyethylene Glycols 3WJQ0SDW1A mehr... carbopol 940 4Q93RCW27E Muramidase EC 3.2.1.17
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245 1 0 |a Complex coacervate core micelles with a lysozyme-modified corona 
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520 |a This paper describes the preparation, characterization, and enzymatic activity of complex coacervate core micelles (C3Ms) composed of poly(acrylic acid) (PAA) and poly(N-methyl-2-vinyl pyridinium iodide)-b-poly(ethylene oxide) (PQ2VP-PEO) to which the antibacterial enzyme lysozyme is end-attached. C3Ms were prepared by polyelectrolyte complex formation between PAA and mixtures containing different ratios of aldehyde and hydroxyl end-functionalized PQ2VP-PEO. This resulted in the formation of C3Ms containing 0-40% (w/w) of the aldehyde end-functionalized PQ2VP-PEO block copolymer (PQ2VP-PEO-CHO). Chemical conjugation of lysozyme was achieved via reductive amination of the aldehyde groups, which are exposed at the surface of the C3M, with the amine groups present in the side chains of the lysine residues of the protein. Dynamic and static light scattering indicated that the conjugation of lysozyme to C3Ms prepared using 10 and 20% (w/w) PQ2VP-PEO-CHO resulted in the formation of unimicellar particles. Multimicellar aggregates, in contrast, were obtained when lysozyme was conjugated to C3Ms prepared using 30 or 40% (w/w) PQ2VP-PEO-CHO. The enzymatic activity of the unimicellar lysozyme-C3M conjugates toward the hydrolysis of the bacterial substrate Micrococcus lysodeikticus was comparable to that of free lysozyme. For the multimicellar particles, in contrast, significantly reduced enzymatic rates of hydrolysis, altered circular dichroism, and red-shifted tryptophan fluorescence spectra were measured. These results are attributed to the occlusion of lysozyme in the interior of the multimicellar conjugates 
650 4 |a Comparative Study 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Acrylic Resins  |2 NLM 
650 7 |a Enzymes, Immobilized  |2 NLM 
650 7 |a Micelles  |2 NLM 
650 7 |a Vinyl Compounds  |2 NLM 
650 7 |a poly(N-methyl-2-vinyl pyridinium iodide)-b-poly(ethylene oxide)  |2 NLM 
650 7 |a Polyethylene Glycols  |2 NLM 
650 7 |a 3WJQ0SDW1A  |2 NLM 
650 7 |a carbopol 940  |2 NLM 
650 7 |a 4Q93RCW27E  |2 NLM 
650 7 |a Muramidase  |2 NLM 
650 7 |a EC 3.2.1.17  |2 NLM 
700 1 |a Klok, Harm-Anton  |e verfasserin  |4 aut 
700 1 |a Norde, Willem  |e verfasserin  |4 aut 
700 1 |a Stuart, Martien A Cohen  |e verfasserin  |4 aut 
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