Large strain response in acceptor- and donor-doped Bi<Subscript>0.5</Subscript>Na<Subscript>0.5</Subscript>TiO<Subscript>3</Subscript>-based lead-free ceramics

Effects of Fe and La addition on the dielectric, ferroelectric, and piezoelectric properties of Bi_0.5Na_0.5TiO₃–Bi_0.5Li_0.5TiO₃–BaTiO₃–Mn ceramics were investigated. Similar to the doping effect in lead-based piezoelectric materials, here the Fe-doped ceramic created a hard effect with an improved mechanical quality factor (Q _m) ~ 160, coercive field (E _c) ~ 2.9 kV/mm, decreased dielectric constant ( e₃₃^T /e₀ ) ~ 80 3, \left( {\varepsilon_{33}^{T} /\varepsilon_{0} } \right)\sim 80 3, and loss (tanδ) ~ 0.024 while the La-doped one indicated a soft feature with improved piezoelectric constant (d ₃₃) ~ 184 pC/N, e₃₃^T /e₀   ~ 983, \varepsilon_{33}^{T} /\varepsilon_{0} \,\sim { 983}, tanδ ~ 0.033, and decreased E _c ~ 2.46 kV/mm. In addition, the temperature dependence of the ferroelectric hysteresis loops and strain response under unipolar electric field was also studied. Around the depolarization temperature T _d, large strain value was obtained with the normalized d₃₃^* d_{33}^{*} up to ~1,000 pC/N, which was suggested originated from the development of the short-range order or non-polar phases in the ferroelectric matrix. All these would provide a new way to realize high piezoelectric response for practical application in different temperature scale.     

Membrane‐Surface Anchoring of Charged Diacylglycerol‐Lactones Correlates with Biological Activities

Synthetic diacylglycerol‐lactones (DAG‐lactones) are effective modulators of critical cellular signaling pathways, downstream of the lipophilic second messenger diacylglycerol, that activate a host of protein kinase C (PKC) isozymes and other nonkinase proteins that share similar C1 membrane‐targeting domains with PKC. A fundamental determinant of the biological activity of these amphiphilic molecules is the nature of their interactions with cellular membranes. This study examines the biological properties of charged DAG‐lactones exhibiting different alkyl groups attached to the heterocyclic nitrogen of an α‐pyridylalkylidene chain, and particularly the relationship between membrane interactions of the substituted DAG‐lactones and their respective biological activities. Our results suggest that bilayer interface localization of the N‐alkyl chain in the R² position of the DAG‐lactones inhibits translocation of PKC isoenzymes onto the cellular membrane. However, the orientation of a branched alkyl chain at the bilayer surface facilitates PKC binding and translocation. This investigation emphasizes that bilayer localization of the aromatic side residues of positively charged DAG‐lactone derivatives play a central role in determining biological activity, and that this factor contributes to the diversity of biological actions of these synthetic biomimetic ligands.