Substantial evidence links α-synuclein, a small highly conserved presynaptic protein with
unknown function, to both familial and sporadic Parkinson's disease (PD). α-Synuclein has …

Proteins can exist in a trinity of structures: the ordered state, the molten globule, and the
random coil. The five following examples suggest that native protein structure can …

The use of curcumin in the food industry is constrained by its poor aqueous dispersibility and
instability. Previous studies have shown that stable curcumin nanoparticles can be prepared …

Developing recombinant protein pharmaceuticals has proved to be very challenging
because of both the complexity of protein production and purification, and the limited …

Noncovalent, extrinsic fluorescent dyes are applied in various fields of protein analysis, eg to
characterize folding intermediates, measure surface hydrophobicity, and detect aggregation …

One of the most challenging tasks in the development of protein pharmaceuticals is to deal
with physical and chemical instabilities of proteins. Protein instability is one of the major …

Binding of the hydrophobia fluorescent probe, 1‐anilino‐naphthalene‐8‐sulfonate (ANS), to
synthetic polypeptides and proteins with a different structural organization has been studied …

Parkinson's disease involves the aggregation of α-synuclein to form fibrils, which are the
major constituent of intracellular protein inclusions (Lewy bodies and Lewy neurites) in …

Structural unfolding of soy protein isolate (SPI) as induced by holding (0, 0.5, 1, 2, and 4 h)
in acidic (pH 1.5− 3.5) and alkaline (pH 10.0− 12.0) pH solutions, followed by refolding (1 h) …

In recent decades, protein-based therapeutics have substantially expanded the field of
molecular pharmacology due to their outstanding potential for the treatment of disease …