Thermally triggered self-assembly of kappa-casein amyloid nanofibrils and their nanomechanical properties
- Authors
- Lee, Jubong; Lee, Ji-Hye; Palk, Seung R.; Yeom, Bongjun; Char, Kookheon
- Issue Date
- Sep-2019
- Publisher
- ELSEVIER SCI LTD
- Keywords
- Amyloids; Self-assembly; Nanomechanical property
- Citation
- POLYMER, v.179, pp.1 - 10
- Indexed
- SCIE
SCOPUS
- Journal Title
- POLYMER
- Volume
- 179
- Start Page
- 1
- End Page
- 10
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/32831
- DOI
- 10.1016/j.polymer.2019.121626
- ISSN
- 0032-3861
- Abstract
- Understanding the self-assembly process of amyloid nanofibrils is important in protein engineering for their potential uses in material sciences and medical applications. Here, we investigated the nanomechanical properties and structures of kappa-casein nanofibrils during thermally induced amyloidogenesis. After treatment with dithiothreitol to reduce disulfide bonds, kappa-casein from bovine milk was incubated at various temperatures from 37 to 95 degrees C. Twisted mature nanofibrils were only obtained at high thermal energies of 95 degrees C with fast growth kinetics. Nanomechanical studies using atomic force microscopy show the highest Young's moduli (2.6 +/- 0.4 GPa) for mature fibrils when compared to those of oligomers and protofibrils (0.6 +/- 0.1 and 2.2 +/- 0.3 GPa, respectively). These enhanced mechanical properties are mainly attributed to the twisted cores of the mature fibrils containing beta-sheet stacks. Amyloidogenesis of kappa-casein is highly dependent on the magnitude of thermal energy, determining both the types and shapes of the nanofibrils and their different mechanical properties.
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