Blue protein with red fluorescence.

The walleye (Sander vitreus) is a golden yellow fish that inhabits the Northern American lakes. The recent sightings of the blue walleye and the correlation of its sighting to possible increased UV radiation have been proposed earlier. The underlying molecular basis of its adaptation to increased UV radiation is the presence of a protein (Sandercyanin)-ligand complex in the mucus of walleyes. Degradation of heme by UV radiation results in the formation of Biliverdin IXα (BLA), the chromophore bound to Sandercyanin. We show that Sandercyanin is a monomeric protein that forms stable homotetramers on addition of BLA to the protein. A structure of the Sandercyanin-BLA complex, purified from the fish mucus, reveals a glycosylated protein with a lipocalin fold. This protein-ligand complex absorbs light in the UV region (λmax of 375 nm) and upon excitation at this wavelength emits in the red region (λmax of 675 nm). Unlike all other known biliverdin-bound fluorescent proteins, the chromophore is noncovalently bound to the protein. We provide here a molecular rationale for the observed spectral properties of Sandercyanin.

In Silico Molecular Docking Studies of Phytocompounds From Coleus Amboinicus Against Glucokinase.

Diabetes is one of the most prevalent metabolic illnesses that can be fatal, and it is the ninth-largest cause of mortality worldwide. Even though there are effective hypoglycemic medications available for the treatment of diabetes, researchers continue to look for a medication that is more effective and has fewer adverse effects by focusing on various metabolic components such as enzymes, transporters, receptors. The enzyme Glucokinase (GCK), which is present mainly in the liver and beta cells of the pancreas, is involved in maintaining blood glucose homeostasis. Hence, the present in silico study is designed to determine the interaction between GCK and compounds (ligands) of Coleus amboinicus. In the current docking investigation, we discovered that important residues, including ASP-205, LYS-169, GLY-181, and ILE-225, significantly influence in ligand binding affinity. Docking tests of these compounds with target proteins revealed that this is a suitable molecule that docks well with the target of diabetes treatment. In conclusion, we believe that the compounds of caryophyllene have anti-diabetic activity based on the present study.