Experimental epidural and conduction anesthesia with azacaine

We present the results of the in vitro action of alpha and gamma interferons and of Intacglobin and Igegam against the 47/93/IPK (Coxsackie A9) strain isolated from the cerebrospinal fluid of a patient with epidemic neuropathy. The in vitro studies showed that the two interferons inhibited the replication of this agent; they also showed the presence of antibodies to it in the Intacglobin and Igegam. The results attained demonstrated that the use of these compounds could be effective for the treatment of this entity.     

Natural Wax for Transient Electronics

Emerging classes of bioresorbable electronic materials serve as the basis for active biomedical implants that are capable of providing sensing, monitoring, stimulating, and other forms of function over an operating period matched to biological processes such as wound healing. These platforms are of interest because subsequent dissolution, enzymatic degradation, and/or bioresorption can eliminate the need for surgical extraction. This report introduces natural wax materials as long‐lived, hydrophobic encapsulation layers for such systems, where biodegradation eventually occurs by chain scission. Studies of wax stability as an encapsulation material demonstrate the ability to retain operation of underlying biodegradable electronic systems for durations between a few days to a few weeks during complete immersion in aqueous solutions in ex‐vivo physiological conditions. Electrically conductive composites result from the addition of tungsten micro/nanoparticles, as a conductive, printable paste with similar lifetimes. Demonstrations of these materials in partially biodegradable wireless light‐emitting diodes and near‐field communication circuits illustrate their use in functional bioresorbable electronic systems. Investigations in animal models reveal no signs of toxicity or other adverse biological responses.     

Tetracyclines induce changes in accessibility of ribosomal proteins to proteases

It is generally assumed that folding intermediates contain partially formed native-like secondary structures. However, if we consider the fact that the conformational stability of the intermediate state is simpler than that of the native state, it would be expected that the secondary structures in a folding intermediate would not necessarily be similar to those of the native state. beta-Lactoglobulin is a predominantly beta-sheet protein, although it has a markedly high intrinsic preference for alpha-helical structure. We have studied the refolding kinetics of bovine beta-lactoglobulin using stopped-flow circular dichroism and find that a partly alpha-helical intermediate accumulates transiently before formation of the native beta-sheets. The present results suggest that the folding reaction of beta-lactoglobulin follows a non-hierarchical mechanism, in which non-native alpha-helical structures play important roles.