Trichogin GA IV (TrGA) is an antimicrobial peptide isolated from Trichoderma longibrachiatum. The amino acid sequence of TrGA is rather peculiar, because it is characterized by three Aib and four Gly residues, which confer unique dynamic and structural properties. In a previous study, we found that TrGA shows excellent binding properties to Ca(II) and lanthanide Gd(III) ions in acetonitrile solutions. Within the lanthanide ions, Tb(III) ions possess fascinating optical characteristics, such as luminescence which greatly improves after coordination. Here, we present the results of our spectroscopic and molecular dynamics investigations on the Tb(III) ion‐binding properties of an Nα‐Fmoc functionalized analog of Trichogin GA IV (F0TrOMe). The high Tb(III) ion‐F0TrOMe affinity, together with the proteolytic resistance and membrane affinity of the natural compound, confers to this system potentially promising applications in several fields, such as bioimaging and bioanalytical assays.

Cellobiose dehydrogenase (CDH) is a fungal extracellular flavocytochrome capable of direct electron transfer (DET). Unlike other CDHs, the pH optimum for CDHs from Corynascus thermophilus (CtCDH) and Humicola insolens (HiCDH) is close to the human physiological pH in blood (7.4). These are, therefore, interesting candidates for glucose measurements in human blood and the application in enzymatic fuel cells is, however, limited by their relatively low activity with this substrate. In this work, the substrate specificities of CtCDH and HiCDH have been altered by a single cysteine to tyrosine substitution in the active sites of CtCDH (position 291) and HiCDH (position 285), which resulted in improved kinetic constants with glucose while decreasing the activity with several disaccharides, including maltose. The DET properties of the generated CDH variants were tested in the absence and in the presence of substrates, on graphite electrodes and thiolic self‐assembled monolayer (SAM)‐modified Au electrodes. Seven different thiols with different spacer lengths were used, containing ‐COOH, ‐OH, and ‐NH2 end groups. The length and head functionality of the thiol govern the efficiency of the DET reaction and indicate different DET properties of CtCDH and HiCDH

The front cover artwork is provided by Prof. Lo Gorton from Lund University (Sweden) and his co‐workers. The image shows mutated cellobiose dehydrogenase (CDH) immobilized on a graphite electrode and how preferentially glucose is oxidized by this enzyme. Read the full text of the Article at 10.1002/celc.201600781.

The Front Cover picture shows mutated cellobiose dehydrogenase (CDH) immobilized on a graphite electrode and how preferentially glucose is oxidized by this enzyme. The enzyme consists of a larger catalytic dehydrogenase domain (grey) containing FAD as cofactor (orange) and a smaller cytochrome domain (lavender) containing heme as cofactor (yellow) connected through a linker region (green). The two electrons transferred from glucose to FAD in the catalytic reaction are then sequentially transferred from FAD to heme and, from there, directly to the electrode in a mediatorless fashion. The CDH in the picture is a mutant specially made to drastically decrease the affinity of the enzyme for maltose to minimize false readout values of blood of diabetic patients. More information can be found in the Article by R. Ortiz, L. Gorton, and co‐workers on page 846 in Issue 4, 2017 (DOI: 10.1002/celc.201600781).