Measurement of the top-Higgs Yukawa coupling at a linear e<Superscript>+</Superscript>e<Superscript>-</Superscript> collider

Understanding the mechanism of electroweak symmetry breaking and the origin of boson and fermion masses is among the most pressing questions raised in contemporary particle physics. If these issues involve one (several) Higgs boson(s), a precise measurement of all its (their) properties will be of prime importance. Among those, the Higgs coupling to matter fermions (the Yukawa coupling). At a linear collider, the process e⁺e^-→tt̄H will allow a direct measurement of the top-Higgs Yukawa coupling. We present a realistic feasibility study of the measurement in the context of the TESLA collider. Four channels are studied and the analysis is repeated for several Higgs mass values within the range 120–200 GeV/c ². PACS 13.66.Jn; 14.65.Ha; 14.80.Bn     

Far infrared optical properties of MoCl5 doped CIS polyacetylene

Far infrared transmission spectra of MoCl₅ homogeneously doped polyacetylene are reported. They show that in this spectral range the optical index is frequency independent but increases strongly with increasing doping level. IR conductivity is compared to d.c. conductivity.     

Nature-inspired dimerization as a strategy to modulate neuropeptide pharmacology exemplified with vasopressin and oxytocin

Vasopressin (VP) and oxytocin (OT) are cyclic neuropeptides that regulate fundamental physiological functions via four G protein-coupled receptors, V_1aR, V_1bR, V₂R, and OTR. Ligand development remains challenging for these receptors due to complex structure–activity relationships. Here, we investigated dimerization as a strategy for developing ligands with novel pharmacology. We regioselectively synthesised and systematically studied parallel, antiparallel and N- to C-terminal cyclized homo- and heterodimer constructs of VP, OT and dVDAVP (1-deamino-4-valine-8-d-arginine-VP). All disulfide-linked dimers, except for the head-to-tail cyclized constructs, retained nanomolar potency despite the structural implications of dimerization. Our results support a single chain interaction for receptor activation. Dimer orientation had little impact on activity, except for the dVDAVP homodimers, where an antagonist to agonist switch was observed at the V_1aR. This study provides novel insights into the structural requirements of VP/OT receptor activation and spotlights dimerization as a strategy to modulate pharmacology, a concept also frequently observed in nature.

Structural and pharmacological study of parallel, antiparallel and N- to C-terminal cyclized homo- and heterodimers of vasopressin and oxytocin. This study spotlights dimerization as a strategy to modulate the pharmacology of neuropeptides.