Tuning Human Serum Albumin (HSA) Hydrogels through Albumin Glycation.

The changes of technological properties of albumin-based hydrogels induced by increasing degrees of post-translational modification of the protein are reported. Maillard-type modification of amino acids arginine and lysine of albumin is achieved through glyoxal as an α-dicarbonyl compound. The degrees of modification are fine-tuned using different molar ratios of glyoxal.

Docking, Synthesis and Evaluation of the Antifungal Activity of Pyrimido [4,5-b]quinolins.

In order to expand the application of FeO@SiO-SnCl in the synthesis of heterocyclic compounds, in this study, we wish to report the use of one-pot three component synthesis of pyrimido [4,5-]quinolone derivatives ( ) through reaction of 6-amino-2-(methylthio)pyrimidin-4 (3)-one, dimedone, or 1,3-cyclohexadione and aldehydes in the presence of FeO@SiO-SnCl as an efficient eco-friendly catalyst under ultrasound irradiation. The final aim of this study is evaluation of antifungal activity of resulted products. Synthesis of pyrimido [4,5-]quinolin derivatives were done three components coupling reaction of aldehyde, dimedone or 1,3-cyclohexadione and 6-amino-2-(methylthio)pyrimidin-4 (3)-one in the presence of FeO@SiO-SnCl under ultrasonic irradiation in water at 60 °C.

Serum albumin hydrogels in broad pH and temperature ranges: characterization of their self-assembled structures and nanoscopic and macroscopic properties.

We report extended pH- and temperature-induced preparation procedures and explore the materials and molecular properties of different types of hydrogels made from human and bovine serum albumin, the major transport protein in the blood of mammals. We describe the diverse range of properties of these hydrogels at three levels: (1) their viscoelastic (macroscopic) behavior, (2) protein secondary structure changes during the gelation process (via ATR-FTIR spectroscopy), and (3) the hydrogel fatty acid (FA) binding capacity and derive from this the generalized tertiary structure through CW EPR spectroscopy. We describe the possibility of preparing hydrogels from serum albumin under mild conditions such as low temperatures (notably below albumin's denaturation temperature) and neutral pH value.