Lactoferrin for the Prevention of Post-antibiotic Diarrhoea

Antibiotic-associated diarrhoea (AAD) is a common cause of morbidity and mortality. Older individuals in long-term care facilities are particularly vulnerable due to multisystem illnesses and the prevailing conditions for nosocomial infections. Lactoferrin, an antimicrobial protein in human breastmilk, was tested to determine whether it would prevent or reduce AAD, including Clostridium difficile in tube-fed long-term care patients. Thirty patients were enrolled in a randomized double-blind study, testing eight weeks of human recombinant lactoferrin compared to placebo for the prevention of antibiotic-associated diarrhoea in long-term care patients. Fewer patients in the lactoferrin group experienced diarrhoea compared to controls (p=0.023). Based on the findings, it is concluded that human lactoferrin may reduce post-antibiotic diarrhoea

Lactoferrin for the Prevention of Post-antibiotic Diarrhoea

Antibiotic-associated diarrhoea (AAD) is a common cause of morbidity and mortality. Older individuals in long-term care facilities are particularly vulnerable due to multisystem illnesses and the prevailing conditions for nosocomial infections. Lactoferrin, an antimicrobial protein in human breastmilk, was tested to determine whether it would prevent or reduce AAD, including Clostridium difficile in tube-fed long-term care patients. Thirty patients were enrolled in a randomized double-blind study, testing eight weeks of human recombinant lactoferrin compared to placebo for the prevention of antibiotic-associated diarrhoea in long-term care patients. Fewer patients in the lactoferrin group experienced diarrhoea compared to controls (p=0.023). Based on the findings, it is concluded that human lactoferrin may reduce post-antibiotic diarrhoea

Where is mineral ballast important for surface export of particulate organic carbon in the ocean?

Correlations between particulate organic carbon (POC) and mineral fluxes in the deep ocean have inspired the inclusion of ‘ballast effect’ parameterizations in carbon cycle models. A recent study demonstrated regional variability in the effect of ballast minerals on the flux of POC in the deep ocean. We have undertaken a similar analysis of shallow export data from the Arctic, Atlantic and Southern Oceans. Mineral ballasting is of greatest importance in the high-latitude North Atlantic, where 60% of the POC flux is associated with ballast minerals. This fraction drops to around 40% in the Southern Ocean. The remainder of the export flux is not associated with minerals, and this unballasted fraction thus often dominates the export flux. The proportion of mineral-associated POC flux often scales with regional variation in export efficiency (the proportion of primary production that is exported). However, local discrepancies suggest that regional differences in ecology also impact the magnitude of surface export. We propose that POC export will not respond equally across all high-latitude regions to possible future changes in ballast availability

Using Covalent Labeling and Mass Spectrometry To Study Protein Binding Sites of Amyloid Inhibiting Molecules

Amyloid aggregates are associated with several debilitating diseases, and there are numerous efforts to develop small molecule treatments against these diseases. One challenge associated with these efforts is determining protein binding site information for potential therapeutics because amyloid-forming proteins rapidly form oligomers and aggregates, making traditional protein structural analysis techniques challenging. Using β-2-microglobulin (β2m) as a model amyloid-forming protein along with two recently identified small molecule amyloid inhibitors (i.e., rifamycin SV and doxycycline), we demonstrate that covalent labeling and mass spectrometry (MS) can be used to map small-molecule binding sites for a rapidly aggregating protein. Specifically, three different covalent labeling reagents, namely diethylpyrocarbonate, 2,3-butanedione, and the reagent pair EDC/GEE, are used together to pinpoint the binding sites of rifamycin SV, doxycycline, and another molecule, suramin, which binds but does not inhibit Cu­(II)-induced β2m amyloid formation. The labeling results reveal binding sites that are consistent with the known effects of these molecules on β2m amyloid formation and are in general agreement with molecular docking results. We expect that this combined covalent labeling approach will be applicable to other protein/small molecule systems that are difficult to study by traditional means