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Layer‐by‐Layer Assembly of κ‐Casein Amyloid Fibrils for the Preparation of Hollow Microcapsules
Author(s) -
Lee Jubong,
Lee JiHye,
Yeom Bongjun,
Char Kookheon
Publication year - 2018
Publication title -
macromolecular chemistry and physics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.57
H-Index - 112
eISSN - 1521-3935
pISSN - 1022-1352
DOI - 10.1002/macp.201700382
Subject(s) - cationic polymerization , biocompatibility , fibril , chemistry , chemical engineering , polymer chemistry , hydrogen bond , layer by layer , amyloid (mycology) , acrylic acid , drug delivery , layer (electronics) , materials science , molecule , organic chemistry , polymer , copolymer , inorganic chemistry , biochemistry , engineering
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.