Proteome analysis of high affinity mouse saliva proteins to hydroxyapatite.

Caries sensitivity varies between the two strains of inbred mice, BALB/cA has high sensitivity and C3H/HeN has low sensitivity. One potential reason seems to be a difference in pellicle-forming saliva protein composition. Here, we performed a proteomic analysis in order to identify differences of hydroxyapatite (HAP) adsorbed saliva proteins between these two mouse strains.

Decrease of laminin-511 in the basement membrane due to photoaging reduces epidermal stem/progenitor cells.

Daily sunlight exposure damages the epidermal basement membrane (BM) and disrupts epidermal homeostasis. Inter-follicular epidermal stem cells (IFE-SCs) regulate epidermal proliferation and differentiation, which supports epidermal homeostasis. Here, we examine how photoaging affects the function of IFE-SCs and we identify key components in their cellular environment (niche).

Heat-induced formation of myosin oligomer-soluble filament complex in high-salt solution.

Heat-induced aggregation of myosin into an elastic gel plays an important role in the water-holding capacity and texture of meat products. Here, we investigated thermal aggregation of porcine myosin in high-salt solution over a wide temperature range by dynamic light scattering experiments. The myosin samples were readily dissolved in 1.

Specific decrease in solution viscosity of antibodies by arginine for therapeutic formulations.

Unacceptably high viscosity is observed in high protein concentration formulations due to extremely large therapeutic dose of antibodies and volume restriction of subcutaneous route of administration. Here, we show that a protein aggregation suppressor, arginine hydrochloride (ArgHCl), specifically decreases viscosity of antibody formulations. The viscosities of bovine gamma globulin (BGG) solution at 250 mg/mL and human gamma globulin (HGG) solution at 292 mg/mL at a physiological pH were too high for subcutaneous injections, but decreased to an acceptable level (below 50 cP) in the presence of 1,000 mM ArgHCl.

Cysteine inhibits the fibrillisation and cytotoxicity of amyloid-β 40 and 42: implications for the contribution of the thiophilic interaction.

Inhibitors of amyloid fibril formation have been at the centre of intense research efforts for the prevention of amyloidosis. Here, we hypothesise that a specific non-covalent interaction, the thiophilic interaction between the side chain of an aromatic residue in a polypeptide and a sulphur atom of the compound, effectively inhibits amyloid fibril formation. Fluorescence spectroscopy and transmission electron microscopy revealed that sulphur compounds, particularly Cys, inhibit the fibrillisation of amyloid-β 1-40 (Aβ40) and 1-42 (Aβ42).

Cysteine inhibits amyloid fibrillation of lysozyme and directs the formation of small worm-like aggregates through non-covalent interactions.

In this article, we discuss the effects of amino acids on amyloid aggregation of lysozyme. l-cysteine (Cys) dramatically inhibited fibrillation of lysozyme, whereas other amino acids (including l-arginine) did not. In the presence of Cys, the aggregation pathway of lysozyme shifted from fibrillation to the formation of the small worm-like aggregates with unfolding.

Arginine and lysine reduce the high viscosity of serum albumin solutions for pharmaceutical injection.

Therapeutic protein solutions for subcutaneous injection must be very highly concentrated, which increases their viscosity through protein-protein interactions. However, maintaining a solution viscosity below 50 cP is important for the preparation and injection of therapeutic protein solutions. In this study, we examined the effect of various amino acids on the solution viscosity of very highly concentrated bovine serum albumin (BSA) and human serum albumin (HSA) at a physiological pH.

Synergistic solubilization of porcine myosin in physiological salt solution by arginine.

Myosin is an important protein resource for food industries and has a bipolar filamentous structure that is composed of subfilaments that occur in vivo. It has been shown that a high ionic strength is required to prevent myosin from forming filamentous structures and to solubilize the protein in aqueous solution. In the presence of 100-200 mM NaCl, 50 mM arginine was more effective than other additives tested, including NaCl, in myosin solubilization.

Effects of alkyl chain length of gallate on self-association and membrane binding.

Alkyl gallates are anticipated for their use as anti-bacterial and anti-viral agents. Although their pharmacological activities depend on their alkyl chain length, no mechanism has yet been clarified. As described herein, we investigated the membrane binding properties of a series of alkyl gallates using fluorescence measurement to elucidate their different pharmacological activities.