Effects of angiotensin II receptor blockers in the coronary arteries of hypertensive rats: Analysis of elemental distribution using LEXRF

Hypertension is one of the major public health problems worldwide. It can cause severely alterations in artery structure and function such as vascular remodeling. Angiotensin II (Ang II) has been linked to vascular dysfunction. It has been shown that blockade of the Ang II type 1 receptor with an Ang II receptor blocker (ARBs) may reverse vascular pathology independently of blood pressure lowering. There is therefore a special interest in establishing whether antihypertensive treatment may correct in part or completely the structural and functional alterations of arteries. Several studies have shown regression of structural remodeling or of functional alterations of small arteries in spontaneously hypertensive rats (SHR) treated with ARBs agents. However, its efficiency was not verified at elemental level in the literature. Knowledge of the elemental distribution in tissues has a great importance in the study of diseases, because chemical imbalance can alter biological functions. Elemental semiquantitative microanalysis in the coronary artery of normotensive, SHRs, and SHRs rats treated with ARBs (losartan and olmesartan) was performed using low energy X-ray fluorescence maps acquired on TwinMic X-ray spectromicroscopy station, located at the Elettra synchrotron radiation facility. Morphological changes in coronary samples were also investigated. The results demonstrate that despite the antihypertensive agents used belong to the same class, their capacities to revert chemical and structural changes in the coronary arteries caused by hypertension are different.     

α‐Aminoxy Oligopeptides: Synthesis,Secondary Structure,and Cytotoxicity of a New Class of Anticancer Foldamers

α‐Aminoxy peptides are peptidomimetic foldamers with high proteolytic and conformational stability. To gain an improved synthetic access to α‐aminoxy oligopeptides we used a straightforward combination of solution‐ and solid‐phase‐supported methods and obtained oligomers that showed a remarkable anticancer activity against a panel of cancer cell lines. We solved the first X‐ray crystal structure of an α‐aminoxy peptide with multiple turns around the helical axis. The crystal structure revealed a right‐handed 2₈‐helical conformation with precisely two residues per turn and a helical pitch of 5.8 Å. By 2D ROESY experiments, molecular dynamics simulations, and CD spectroscopy we were able to identify the 2₈‐helix as the predominant conformation in organic solvents. In aqueous solution, the α‐aminoxy peptides exist in the 2₈‐helical conformation at acidic pH, but exhibit remarkable changes in the secondary structure with increasing pH. The most cytotoxic α‐aminoxy peptides have an increased propensity to take up a 2₈‐helical conformation in the presence of a model membrane. This indicates a correlation between the 2₈‐helical conformation and the membranolytic activity observed in mode of action studies, thereby providing novel insights in the folding properties and the biological activity of α‐aminoxy peptides.     

Highly Selective Removal of Perfluorinated Contaminants by Adsorption on All‐Silica Zeolite Beta

Perfluorinated alkylated substances (PFASs) are widely used in industrial and commercial applications, leading to a widespread occurrence of these persistent and harmful contaminants in our environment. Removal of these compounds from surface and waste waters is being mandated by European and U.S. governments. Currently, there are no treatment techniques available that lower the concentrations of these compounds for large water bodies in a cost‐ and energy‐efficient way. We hereby propose a hydrophobic, all‐silica zeolite Beta material that is a highly selective and high‐capacity adsorbent for PFASs, even in the presence of organic competitors. Advanced characterization data demonstrate that the adsorption process is driven by a very negative adsorption enthalpy and favorable steric factors.