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Micelle formation is an intricate process that hinges on the properties of amphiphilic or amphipathic molecules and the conditions of the system in which they are found. Amphiphilic molecules, which have both hydrophilic (water-attracting) and hydrophobic (water-repelling) parts, play a critical role in this process.In aqueous environments, these molecules arrange themselves such that their hydrophilic heads are turned towards the water phase, while their hydrophobic tails are oriented away...
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Assembly and Characterization of Polyelectrolyte Complex Micelles
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Published on: March 2, 2020

Complex coacervate core micelles with a lysozyme-modified corona.

Maarten Danial1, Harm-Anton Klok, Willem Norde

  • 1Laboratory for Physical Chemistry and Colloid Science, Wageningen University, Dreijenplein 6, 6703 HB Wageningen, The Netherlands.

Langmuir : the ACS Journal of Surfaces and Colloids
|June 23, 2007
PubMed
Summary

This study developed enzyme-conjugated nanoparticles called complex coacervate core micelles (C3Ms). Unimicellar C3Ms retained lysozyme enzyme activity, while multimicellar structures showed reduced activity due to enzyme occlusion.

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Preparation and Characterization of Individual and Multi-drug Loaded Physically Entrapped Polymeric Micelles

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Area of Science:

  • Polymer Science and Engineering
  • Biomaterials Science
  • Enzyme Engineering

Background:

  • Complex coacervate core micelles (C3Ms) offer a versatile platform for encapsulating and functionalizing biomolecules.
  • End-attachment of enzymes like lysozyme to nanostructures is crucial for targeted delivery and enhanced therapeutic efficacy.
  • Controlling the morphology of C3Ms (unimicellar vs. multimicellar) is key to preserving enzyme activity.

Purpose of the Study:

  • To prepare and characterize lysozyme-conjugated C3Ms using poly(acrylic acid) (PAA) and functionalized poly(N-methyl-2-vinyl pyridinium iodide)-b-poly(ethylene oxide) (PQ2VP-PEO).
  • To investigate the impact of C3M morphology on the enzymatic activity of the end-attached lysozyme.
  • To explore the potential of C3Ms as carriers for antibacterial enzymes.

Main Methods:

  • Preparation of C3Ms via polyelectrolyte complexation between PAA and varying ratios of aldehyde-functionalized PQ2VP-PEO (PQ2VP-PEO-CHO).
  • Conjugation of lysozyme to C3Ms using reductive amination of surface-exposed aldehyde groups.
  • Characterization of particle size and morphology using dynamic and static light scattering.
  • Assessment of enzymatic activity against Micrococcus lysodeikticus and analysis of structural changes (circular dichroism, fluorescence spectroscopy).

Main Results:

  • Lysozyme conjugation to C3Ms with 10-20% PQ2VP-PEO-CHO yielded unimicellar particles.
  • C3Ms with 30-40% PQ2VP-PEO-CHO formed multimicellar aggregates upon lysozyme conjugation.
  • Unimicellar lysozyme-C3M conjugates exhibited enzymatic activity comparable to free lysozyme.
  • Multimicellar conjugates showed significantly reduced enzymatic rates, altered circular dichroism, and red-shifted fluorescence, indicating enzyme occlusion.

Conclusions:

  • The morphology of C3Ms critically influences the accessibility and activity of the end-attached lysozyme.
  • Unimicellar C3M architecture preserves lysozyme enzymatic function, suggesting suitability for antibacterial applications.
  • Multimicellar aggregation leads to enzyme occlusion and loss of activity, highlighting the importance of structural control in C3M design.