lactoferrin and maltodextrin

The use of oral rehydration solution (ORS) has revolutionized the management of acute diarrhea. The implementation of the standard World Health Organization ORS (WHO-ORS) has resulted in decreased mortality associated with acute diarrheal illnesses in children, although in general stool volume and diarrhea durations are not reduced. Decreased morbidity and mortality have occurred because of improved hydration status. Decreased morbidity has also been described in adults who used this therapy. Various modifications to the standard ORS have been derived. These modifications have included hypo-osmolar or hyperosmolar solutions, use of rice-based ORS, zinc supplementation, and the use of amino acids, including glycine, alanine, and glutamine. Some of these variations have been successful, some have not, and others are still under investigation. ORS has been used for travelers' diarrhea and to decrease intravenous (IV) fluid requirements in patients with short bowel syndrome (SBS) who require parenteral nutrition (PN). This paper reviews the standard WHO-ORS and its mechanism of action, followed by more contemporary reduced osmolarity ORS and rice-based ORS in non-cholera diarrhea. Various modifications to improve ORS are also discussed.

Topics: Amino Acids; Animals; Bicarbonates; Clinical Trials as Topic; Diarrhea; Flavoring Agents; Fluid Therapy; Glucose; Humans; Lactoferrin; Muramidase; Oryza; Osmolar Concentration; Polysaccharides; Potassium Chloride; Sodium Chloride; Zinc

There is an increasing dataset of solved biomolecular structures in more than one conformation and increasing evidence that large-scale conformational change is critical for biomolecular function. In this article, we present our implementation of a dynamic importance sampling (DIMS) algorithm that is directed toward improving our understanding of important intermediate states between experimentally defined starting and ending points. This complements traditional molecular dynamics methods where most of the sampling time is spent in the stable free energy wells defined by these initial and final points. As such, the algorithm creates a candidate set of transitions that provide insights for the much slower and probably most important, functionally relevant degrees of freedom. The method is implemented in the program CHARMM and is tested on six systems of growing size and complexity. These systems, the folding of Protein A and of Protein G, the conformational changes in the calcium sensor S100A6, the glucose-galactose-binding protein, maltodextrin, and lactoferrin, are also compared against other approaches that have been suggested in the literature. The results suggest good sampling on a diverse set of intermediates for all six systems with an ability to control the bias and thus to sample distributions of trajectories for the analysis of intermediate states.

Topics: Algorithms; Animals; Calcium-Binding Proteins; Cell Cycle Proteins; Humans; Lactoferrin; Molecular Dynamics Simulation; Monosaccharide Transport Proteins; Nerve Tissue Proteins; Periplasmic Binding Proteins; Polysaccharides; Protein Conformation; Protein Folding; Proteins; S100 Calcium Binding Protein A6; S100 Proteins; Staphylococcal Protein A; Thermodynamics