Zn(II)-alloferon complexes - Similar sequence, different coordination modes, no antibacterial activity.
Often, in the search for a highly defined scientific phenomenon, a different one becomes apparent. This was also the case of this work, in the scope of which we planned to search for metal-enhanced, novel antibacterial/ antifungal compounds. Instead, we denied the existence of such and revealed the details of the bioinorganic chemistry of Zn(II)-alloferon complexes. Zinc(II) complexes of alloferon 1 and 2, ligands with a sequential difference of one amino acid only, show a substantially different coordination pattern at physiological pH. In the case of Zn(II)-alloferon 1 species, a histamine-like binding mode is observed (N-terminal amine and imidazole of His-1) and the coordination sphere …
Thermodynamic surprises of Cu(II)–amylin analogue complexes in membrane mimicking solutions
AbstractMembrane environment often has an important effect on the structure, and therefore also on the coordination mode of biologically relevant metal ions. This is also true in the case of Cu(II) coordination to amylin analogues—rat amylin, amylin1–19, pramlintide and Ac-pramlintide, which offer N-terminal amine groups and/or histidine imidazoles as copper(II) anchoring sites. Complex stabilities are comparable, with the exception of the very stable Cu(II)–amylin1–19, which proves that the presence of the amylin C-terminus lowers its affinity for copper(II); although not directly involved, its appropriate arrangement sterically prevents early metal binding. Most interestingly, in membrane…
Pneumococcal HxxHxH triad – Copper(II) interactions – How important is the ‘x’?
Abstract PhtA, a Streptococcus pneumoniae polyhistidine triad protein, which contributes to virulence by interacting with components of the immune system, by being involved in adherence of bacteria and in Zn(II) uptake, contains five copies of the HxxHxH sequence. Since this motif is also present in numerous Cu(II) binding proteins, we decided to focus on the bioinorganic chemistry of copper(II) with three of such PhtA repeats, in order to understand which of the PhtA triads binds Cu(II) with the highest affinity and explain if Cu(II) would be able to outcompete Zn(II) from its native binding site under physiological metal concentrations.
Variation in predation risk and vole feeding behaviour: a field test of the risk allocation hypothesis.
Many prey animals experience temporal variation in the risk of predation and therefore face the problem of allocating their time between antipredator efforts and other activities like feeding and breeding. We investigated time allocation of prey animals that balanced predation risk and feeding opportunities. The predation risk allocation hypothesis predicts that animals should forage more in low- than in high-risk situations and that this difference should increase with an increasing attack ratio (i.e. difference between low- and high-risk situations) and proportion of time spent at high risk. To test these predictions we conducted a field test using bank voles ( Clethrionomys glareolus) as…
Pneumococcal histidine triads – involved not only in Zn2+, but also Ni2+ binding?
Polyhistidine triad proteins, which participate in Zn2+ uptake in Streptococcus pneumoniae, contain multiple copies of the HxxHxH (histidine triad motif) sequence. We focus on three such motifs from one of the most common and well-conserved polyhistidine triad proteins, PhtA, in order to understand their bioinorganic chemistry; particular focus is given to (i) understanding which of the PhtA triads binds Zn2+ with the highest affinity (and why) and (ii) explaining whether Ni2+ (also crucial for bacterial survival and virulence) could potentially outcompete Zn2+ at its native binding site. There is no significant difference in the stability of zinc(II) complexes with the three studied protei…
Zinc(II)—The Overlooked Éminence Grise of Chloroquine’s Fight against COVID-19?
The authors would like to thank Agnieszka Michalczuk for providing us with her artistic vision of SARS-CoV-2.