The development of specialized nanoparticles for use in the detection and treatment of cancer is increasing. Methods are being proposed and tested that could target treatments more directly to cancer cells, which could lead to higher efficacy and reduced toxicity, possibly even eliminating the adverse effects of damage to the immune system and the loss of quick replicating cells. In this mini-review we focus on recent studies that employ folate nanoconjugates to target the folate receptor. Folate receptors are highly overexpressed on the surface of many tumor types. This expression can be exploited to target imaging molecules and therapeutic compounds directly to cancerous tissues.

Moonlighting proteins comprise a class of multifunctional proteins in which a single polypeptide chain performs multiple biochemical functions that are not due to gene fusions, multiple RNA splice variants or pleiotropic effects. The known moonlighting proteins perform a variety of diverse functions in many different cell types and species, and information about their structures and functions is scattered in many publications. We have constructed the manually curated, searchable, internet-based MoonProt Database (http://www.moonlightingproteins.org) with information about the over 200 proteins that have been experimentally verified to be moonlighting proteins. The availability of this organized information provides a more complete picture of what is currently known about moonlighting proteins. The database will also aid researchers in other fields, including determining the functions of genes identified in genome sequencing projects, interpreting data from proteomics projects and annotating protein sequence and structural databases. In addition, information about the structures and functions of moonlighting proteins can be helpful in understanding how novel protein functional sites evolved on an ancient protein scaffold, which can also help in the design of proteins with novel functions.

No abstract

Laminaripentaose-producing b-1,3-glucanase (LPHase) catalyzes the hydrolysis of a long chain polysaccharide b-1,3-glucan into specific pentasaccharide oligomers. LPHase is a member of the glycoside hydrolase family 64 (GH-64) that play important roles during biomass degradation. Experimentally, the enzymatic mechanism of LPHase remains to be determined although it has been reported that Glu154 and Asp170 may serve as the active site residues of LPHase. Molecular modelling may offer more insight into the reaction pathway. Several synthetic substrates of LPHase have been reported. We chose laminarihexaose as the substrate and docked one structure of laminarihexaose obtained from the Protein Data bank to the active site of LPHase. Molecular dynamics simulations using a combined quantum mechanical and molecular mechanical (QM/MM) method have been employed to study the hydrolysis of the glycosidic bond catalyzed by LPHase. Our results on the current LPHase-substrate complex suggest that the proton transfer from the catalytic general acid to the glycosidic oxygen be concerted with the nucleophilic attack at the anomeric carbon, and the free energy of activation is about 30 kcal/mol. Additional simulations on LPHase-substrate complexes are underway to characterize the LPHase catalyzed reaction pathway.