Amyloid-like aggregation of bovine serum albumin at physiological temperature induced by cross-seeding effect of HEWL amyloid aggregates

Deciphering Dual Modes of Parkinsonian Biomolecules Derived Fluorescent Nanoparticles: Protein Specificity and White Light Generation

“…Finally, the involvement of the globular albumin protein BSA among all the other used proteins in the most prominent interaction with the synthesized fluorescent NPs as well as in the most efficient WL emission generation has influenced us to explore the NP interaction and Dox mediated WL emission generation in the presence of BSA fibrils. BSA or serum albumin protein is one of the most abundant and physiologically important protein molecules, and under a proper synthetic approach it transformed into fibril aggregates, which can be employed as a model system for amyloid based studies of different neurodegenerative as well as metabolic disorders. , The synthesis of rigid BSA fibrils has been performed following the reported work of Usov et al in a salt free environment (to avoid any kind of interference due to salt) and elaborated as well as illustrated (Scheme S3) in the Supporting Information. The synthesized rigid fibril assemblies have been characterized using scanning electron microscopy (SEM) and AFM images, are been shown in Figure S12a and b, respectively.…”

In Vitro Interaction of a C-Terminal Fragment of TDP-43 Protein with Human Serum Albumin Modulates Its Aggregation

“…As the aggregation kinetics of TDP-43 2C in the presence of HSA was observed to be different with the elimination of the lag phase, we further examined the difference in the sarkosyl detergent stability of aggregates of TDP-43 2C formed alone versus in the presence of HSA. Notably, the stability of amyloid-like aggregates of proteins can be enhanced against ionic detergents such as SDS and sarkosyl based on the conformation and aggregation patterns of amyloid aggregates. , In earlier studies, it had been shown that the TDP-43 2C aggregates exhibit partial resistance against dis-aggregation by sarkosyl . Therefore, we assessed the TDP-43 2C aggregates’ stability formed in the presence and absence of HSA by treating all the 15 h incubated samples with 1% sarkosyl at room temperature followed by electrophoresis on 1% agarose gel.…”

“…All the samples were incubated at room temperature with 1% sarkosyl for 10 min and then added with nonreducing Laemmli sample buffer. Samples were then loaded into the wells, and electrophoresis was performed on 1% agarose gel for 60 min at 90 V. 49,50 Then, the protein from the gel was electroblotted to PVDF membrane using a semidry transfer cell for 70 min at 25 V. After the transfer, the membrane was overnight blocked by using casein blocking buffer followed by a wash using PBS-…”

Nutrient‐sensing amyloid metastasis

“…Amyloid fibrils are not exclusive features of diseaserelated proteins. In fact, a large variety of polypeptides of unknown biological relevance can also form amyloid structures, 19 such as non-natural small peptides fragments, 20,21 peptide-nucleic acid hybrids, 22 long polyaminoacids, 23 apomyolglobin, 24 apohemoglobin, 25 albumin, 26,27 casein, 28,29 β-lactoglobulin, 30 hen egg white lysozyme, 31,32 insulin, 33 glucagon, 34 growth hormone, 35 pramlintide, 36,37 among others. Such typical folding pattern is indicative of amyloid as highly organized, common structural arrangement, which may be populated under a particular circumstance, triggering such common supramolecular folding pattern.…”

“…41,58,[60][61][62][63] Furthermore, the general cross-seeding nature of amyloid structures regardless of the polypeptide sequence has emerged, 45,48 with the perspective of a given amyloid material to work as self-and cross-replicating accessory protein-either as a scaffold 58,63 or as a co-amyloid, participating in an heterologous amyloid product. 27,[64][65][66][67] Amyloid proteins can thus perform homo-or heterointeraction with other proteins, co-opting them as clients.…”