Abstract
The fabrication of amyloid-based hydrogels has attracted remarkable attention within the field of materials science and technology. These materials have a multitude of potential applications in the biomaterials field such as developing scaffolds for tissue engineering, drug delivery and hygiene products. Despite the potential new applications of these materials, the physical nature of their assembly is not well understood. In this study, we have investigated how the conformation of the amyloid precursor state (I) is formed and correlated with the assembly of amyloid-based hydrogels. A transparent hydrogel was fabricated at pH 7.4 by cooling of the temperature-induced unfolded state of hen egg white lysozyme (HEWL). The completely unfolded state (U) at the gelation concentration of HEWL was obtained around 90 °C in the presence of tris(2-carboxyethyl)phosphine (TCEP), with a TCEP/HEWL molar ratio of 4 : 1. The characterization of the hydrogel showed that it was composed of an amyloid fibril-like material. The physical nature of its assembly was examined in detail and it was found that the hydrogel formation reaction was a three-step, four-states process (U → I → F → H). We concluded that the properties of the pre-molten globule state (I) of the protein correlated only with the fibrillation process, whereas the assembly of the fibrils into an hydrogel was found to be almost independent of the I state. Thus, the study presented here provides a complete biophysical insight into the pathway of lysozyme hydrogel assembly.
Highlights
The self-assembly of proteins and peptides into amyloid-like brils is mainly known for its notorious role in many pathological conditions such as Alzheimer's disease, Parkinson's disease, and type II diabetes.[1]
We found that hen egg white lysozyme (HEWL) at protein concentrations $300 mM preincubated with TCEP in a TCEP/HEWL molar ratio of 4 : 1 and heated at 90 C, converted into a self-healing hydrogel immediately a er cooling the solution to 25 C
HEWL (700 mM) samples preincubated with different concentrations of TCEP at pH 7.4 were heated at six different temperatures ranging from 40 C to 90 C
Summary
The self-assembly of proteins and peptides into amyloid-like brils is mainly known for its notorious role in many pathological conditions such as Alzheimer's disease, Parkinson's disease, and type II diabetes.[1] protein brils are known to play functional roles in many organisms, including bacteria, yeasts and humans.[1,2] Since amyloid-like brils have been found to possess remarkable stability, tensile strength and tunable physicochemical properties, they can be fabricated into smart materials for various bio-nanotechnological applications.[3,4] Amyloid-based hydrogels (AbHs) are one of such smart materials and are very useful for various biomedical and nanotechnological applications.[5,6,7]. Amyloid-based hydrogels (AbHs) are water-laden, threedimensional materials formed by cross-linking of protein brils. The ability of AbHs to hold large amounts of water comes from the fact that they have a large number of hydrophilic functional groups present in their polymeric chains.
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