4 years ago

Layer-by-Layer Assembly of κ-Casein Amyloid Fibrils for the Preparation of Hollow Microcapsules

Layer-by-Layer Assembly of κ-Casein Amyloid Fibrils for the Preparation of Hollow Microcapsules
Ji-Hye Lee, Bongjun Yeom, Kookheon Char, Jubong Lee
Amyloids are known to self-assemble into fibril forms derived from natural or artificial proteins exhibiting superior mechanical properties, stability, and biocompatibility. However, few studies have investigated the applications of amyloid fibrils. Herein, the layer-by-layer growth of zwitterionic κ-casein amyloid fibrils (κCFs) to prepare stable hollow microcapsules is investigated, which is potentially applicable to drug delivery systems. The growth of κCFs increases linearly when electrostatic interactions between the constituent pair become more prominent, for instance, cationic κCFs paired with poly(sodium 4-styrenesulfonate) (PSS), and anionic κCFs paired with poly(diallyldimethylammonium chloride). In contrast, the increase in film thickness shows the exponential-to-linear transition when hydrogen bonding is responsible for adsorption between cationic κCFs and poly(acrylic acid) (PAA). It is thus concluded that stable κCF/PSS hollow microcapsules are prepared by using the electrostatic interaction. However, the κCF/PAA hollow microcapsules are ruptured due to the breakage of hydrogen bonding upon removal of sacrificial templates. The growth and surface morphology of the layer-by-layer-assembled films are explored, consisting of zwitterionic κ-casein amyloid fibrils (κCF) depending on the types of intermolecular interactions. Stable and mechanically robust κCF/poly(sodium 4-styrenesulfonate) hollow microcapsules are only possible with the electrostatic interactions, while κCF/poly(acrylic acid) samples are ruptured due to the breakage of hydrogen bonding during the removal of sacrificial templates.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/macp.201700382

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