Pattern Switching Compact Patch Antenna for On-body and Off-body Communications at 2.45 GHz

The ability to switch between propagating modes is important for body-centric applications such as medical body area networks where a single node may need to be able to optimise communications for either on-body sensor links or off-body links to the wider network. Therefore, we present a compact 2.45 GHz active mode-switching wearable antenna for both on-body and off-body wireless communications. The single-layer patch antenna was pattern-switched using shorting pins and had an impedance bandwidth of 253 MHz and 217 MHz for the on-body and off-body radiating modes, respectively. An efficiency of 57 % and 56.8 % was obtained for on-body and off-body mode respectively when placed in close proximity to a phantom that represents a muscle issue at 2.45 GHz.

A Modified Pole-Zero Technique for the Synthesis of Waveguide Leaky-Wave Antennas Loaded With Dipole-Based FSS

An extension of the pole-zero matching method proposed by Stefano Maci et al. for the analysis of electromagnetic bandgap (EBG) structures composed by lossless dipole-based frequency selective surfaces (FSS) printed on stratified dielectric media, is presented in this paper. With this novel expansion, the dipoles length appears as a variable in the analytical dispersion equation. Thus, modal dispersion curves as a function of the dipoles length can be easily obtained with the only restriction of single Floquet mode propagation. These geometry-dispersion curves are essential for the efficient analysis and design of practical EBG structures, such as waveguides loaded with artificial magnetic conductors (AMC) for miniaturization, or leaky-wave antennas (LWA) using partially reflective surfaces (PRS). These two practical examples are examined in this paper. Results are compared with full-wave 2D and 3D simulations showing excellent agreement, thus validating the proposed technique and illustrating its utility for practical designs.

A distributed contention-vector division multiple access (D-CVDMA) protocol for wireless networks

Traditional Time Division Multiple Access (TDMA) protocol provides deterministic periodic collision free data transmissions. However, TDMA lacks flexibility and exhibits low efficiency in dynamic environments such as wireless LANs. On the other hand contention-based MAC protocols such as the IEEE 802.11 DCF are adaptive to network dynamics but are generally inefficient in heavily loaded or large networks. To take advantage of the both types of protocols, a D-CVDMA protocol is proposed. It is based on the k-round elimination contention (k-EC) scheme, which provides fast contention resolution for Wireless LANs. D-CVDMA uses a contention mechanism to achieve TDMA-like collision-free data transmissions, which does not need to reserve time slots for forthcoming transmissions. These features make the D-CVDMA robust and adaptive to network dynamics such as node leaving and joining, changes in packet size and arrival rate, which in turn make it suitable for the delivery of hybrid traffic including multimedia and data content. Analyses and simulations demonstrate that D-CVDMA outperforms the IEEE 802.11 DCF and k-EC in terms of network throughput, delay, jitter, and fairness.

Identification of Determinants of Glucose-Dependent Insulinotropic Polypeptide Receptor That Interact with N-Terminal Biologically Active Region of the Natural Ligand

Glucose-dependent insulinotropic polypeptide receptor (GIPR), a member of family B of the G-protein coupled receptors, is a potential therapeutic target for which discovery of nonpeptide ligands is highly desirable. Structure-activity relationship studies indicated that the N-terminal part of glucose-dependent insulinotropic polypeptide (GIP) is crucial for biological activity. Here, we aimed at identification of residues in the GIPR involved in functional interaction with N-terminal moiety of GIP. A homology model of the transmembrane core of GIPR was constructed, whereas a three-dimensional model of the complex formed between GIP and the N-terminal extracellular domain of GIPR was taken from the crystal structure. The latter complex was docked to the transmembrane domains of GIPR, allowing in silico identification of putative residues of the agonist binding/activation site. All mutants were expressed at the surface of human embryonic kidney 293 cells as indicated by flow cytometry and confocal microscopy analysis of fluorescent GIP binding. Mutation of residues Arg183, Arg190, Arg300, and Phe357 caused shifts of 76-, 71-, 42-, and 16-fold in the potency to induce cAMP formation, respectively. Further characterization of these mutants, including tests with alanine-substituted GIP analogs, were in agreement with interaction of Glu3 in GIP with Arg183 in GIPR. Furthermore, they strongly supported a binding mode of GIP to GIPR in which the N-terminal moiety of GIP was sited within transmembrane helices (TMH) 2, 3, 5, and 6 with biologically crucial Tyr1 interacting with Gln224 (TMH3), Arg300 (TMH5), and Phe357 (TMH6). These data represent an important step toward understanding activation of GIPR by GIP, which should facilitate the rational design of therapeutic agents.