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    In Situ Fibril Formation of κ-Casein by External Stimuli within Multilayer Thin Films

    Year: 2013

    Journal: ACS Macro Lett., 2013, 2 (8), pp 688–693, 20131001

    Authors: Ji-Hye Lee 1 2, Hyun Joo Hwang 1, Ghibom Bhak 2, Yeongseon Jang 1 2, Seung R. Paik 2, and Kookheon Char *1 2

    Last authors: Kookheon Char

    Organizations: 1 The National Creative Research Initiative Center for Intelligent Hybrids, The WCU Program of Chemical Convergence for Energy & Environment, korea 2 School of Chemical & Biological Engineering, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-744, Korea

    Country: Korea

    We have developed the in situ fibrillation of κ-casein, employed as amyloid precursor, within multilayer films consisting of κ-casein and poly(acrylic acid) (PAA) prepared by the layer-by-layer (LbL) deposition. The fibrillation of κ-casein within the multilayered films is strongly dependent on the extent of intermolecular interactions between κ-casein and PAA. When films constructed initially at pH 3 were heat treated at the same pH, κ-casein did not transform into fibrils. However, when the films were subjected to heat treatment at pH 5, κ-casein was transformed into fibrils within multilayer films due to weakened intermolecular interactions between κ-casein and PAA. We also noted that the multilayer film was swollen at pH 5 by the charge imbalance within the film, which we believe gives enough mobility for κ-caseins to form fibrils with adjacent κ-caseins within the multilayer. The fibrils were found to be uniformly distributed across the entire film thickness, and the aspect ratio as well as the number density of fibrils increased as a function of incubation time. The present study reveals a strategy to realize in situ nanocomposites within LbL multilayer films simply by triggering the formation of protein fibrils by controlling the intermolecular interactions between amyloid precursors and polyelectrolytes (PEs).