Dynamic Properties of Adsorption Layers of κ-Casein Fibrils

Milyaeva, Olga Yu.; Akentiev, Alexander V.; Bykov, Alexey G.; Loglio, Giuseppe; Miller, Reinhard; Portnaya, Irina; Rafikova, Anastasiya R.; Noskov, Boris A.

doi:10.1021/acs.langmuir.3c01950

Cited by 1 publication

(1 citation statement)

References 56 publications

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“…Removing the residual peptide from formed nanofibrils may improve the cross-sectional moment of inertia, the elastic modulus, and bending rigidity . It will also improve the interfacial property of amyloid fibrils, such as interfacial yield strain and surface elasticity, which are crucial for emulsion stabilization . From a biological perspective, some peptides that might trigger allergic reactions can be removed .…”

Section: Processing Methodsmentioning

confidence: 99%

From Fundamental Amyloid Protein Self-Assembly to Development of Bioplastics

Li,

Kambanis,

Sorenson

et al. 2023

Biomacromolecules

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Proteins can self-assemble into a range of nanostructures as a result of molecular interactions. Amyloid nanofibrils, as one of them, were first discovered with regard to the relevance of neurodegenerative diseases but now have been exploited as building blocks to generate multiscale materials with designed functions for versatile applications. This review interconnects the mechanism of amyloid fibrillation, the current approaches to synthesizing amyloid protein-based materials, and the application in bioplastic development. We focus on the fundamental structures of self-assembled amyloid fibrils and how external factors can affect protein aggregation to optimize the process. Protein self-assembly is essentially the autonomous congregation of smaller protein units into larger, organized structures. Since the properties of the self-assembly can be manipulated by changing intrinsic factors and external conditions, protein self-assembly serves as an excellent building block for bioplastic development. Building on these principles, general processing methods and pathways from raw protein sources to mature state materials are proposed, providing a guide for the development of large-scale production. Additionally, this review discusses the diverse properties of protein-based amyloid nanofibrils and how they can be utilized as bioplastics. The economic feasibility of the protein bioplastics is also compared to conventional plastics in large-scale production scenarios, supporting their potential as sustainable bioplastics for future applications. P lastics are now found in every sector of our life, such as packaging, personal care products, electronics, and clothing, while the contamination caused by the accumulation of single-use plastic 1−5 and microplastics 6,7 has become a serious threat to the natural environment, wildlife, and humans. Current plastics can be classified based on their source and their biodegradability, as shown in Figure 1. 8 Some plastics are

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