Abstract: The invention provides an ultrasound patch (710) comprising a first array group (720) comprising a primary transducer array (730) having a first orientation and a second array group (740) comprising at least two secondary transducer arrays (750) each having an orientation different from the first orientation. The second array group is arranged such that the at least two secondary transducer arrays are located at either side of the primary transducer array. The first array group or the second array group may be used to capture preliminary ultrasound data for positioning the ultrasound patch. The primary transducer array and the at least two secondary transducer arrays may comprise CMUTs, and the ultrasound patch may comprise a flip chip connection. Also disclosed are a system and a method for positioning the ultrasound patch on a surface of a subject.

Abstract: A new family Here we report a new family of four-cystine/three-loop conotoxins (designated framework 14). Three peptides of this family (flf14a-c) were isolated from the venom of Conus floridanus floridensis and one (vil14a) from the venom of Conus villepinii, two worm-hunting Western Atlantic cone snail species. CD spectra and nanoNMR spectroscopy of these conotoxins directly isolated from the cone snails revealed a highly helical secondary structure for the four conotoxins. Sequence-specific nanoNMR analysis at room temperature revealed a well-defined helix-loop-helix tertiary structure that resembles that of the Cs ?/? scorpion toxins ?-hefutoxin, ?-KTx1.3 and Om-toxins, which adopt a stable three-dimensional fold where the two ?-helices are linked by the two disulfide bridges. One of these conotoxins (vil14a) has a Lys/Tyr (or Phe) diad, separated by approximately 6 ?, which is a conserved structural feature in K+ channel blockers.

Abstract: Isolation, synthesis and therapeutic use of conotoxin and conophan compounds and related compositions including a new class of conopeptides including the modified amino acid D-?-hydro-oxyvalinie (D-Hyv=V*) are described herein. These isolated peptides are the first known example of a naturally occurring polypeptide chain containing D-Hyv. The active peptides, termed ?-Hydroxyconophans are heavily hydroxylated small peptides. These peptides contain a definitive structural motif which is a double modification of the polypeptide chain (?-D-OH-Hyv-Trp).

Abstract: Isolation, synthesis and therapeutic use of compounds and related compositions based on a new class of conopeptides comprising the modified amino acid ?-hydroxyvaline (Hyv=V*). These isolated peptides are the first known example of a naturally occurring polypeptide chain containing Hyv. The active peptides, termed ?-Hydroxyconophans are heavily hydroxylated small peptides. These peptides contain a definitive structural motif which is a double modification of the polypeptide chain (?-OH-Hyv-D-Trp).

Abstract: Disclosed are methods and compositions for modulation of ion levels in cells. The compositions contain a new class of biologically active peptides derived from the venom of predatory marine snails of the species Conus gladiator and Conus mus. The active peptides, termed &ggr;-Hydroxyconophans are heavily hydroxylated small peptides. These peptides contain a definitive structural motif which is a double modification of the polypeptide chain in contiguous residues, i.e., &ggr;-OH-Hyv-D-Trp.