Cine magnetic resonance imaging study of blood flow and wall motion of the aortic arch

The aortic arch has 3D distortions in the transverse arch in the axial view, and we previously reported that this distortion is a risk factor in the pathogenesis of arch aneurysms. In this study, we evaluated blood flow and movement of the aortic arch. In 10 healthy young volunteers, ECG-gated cine magnetic resonance imaging was carried out in the axial plane of the transverse arch, the coronal plane of the ascending arch, and the long axial plane along the entire arch. 1. Left anterolateral movements around the midpoint of the transverse arch in the systolic phase were observed in all of the men (6.3 +/- 1.59 mm) and women (4.8 +/- 0.73 mm). 2. A jet flow was detected in the systolic phase along the right side of the aortic wall. At the top of the plane, this jet flow turned to the left in a clockwise rotation in the anterior view. 3. In the long axial plane, a turbulent flow in the systolic phase was observed distal to the left subclavian arterial orifice in 6 of the 7 cases. In conclusion, this turbulent flow and left anterolateral wall motion of the transverse arch are due to anatomical three-dimensional distortion of the transverse arch. We propose that these phenomena may be important risk factors in the pathogenesis of arch aneurysms.     

Structure effects of double D-amino acid replacements: a nuclear magnetic resonance and circular dichroism study using amphipathic model helices

D-Amino acid replacements and the determination of resulting structural changes are a useful tool to recognize amphipathic helices in biologically active peptides such as neuropeptide Y and corticotropin-releasing factor. In this paper the secondary structures of one amphipathic alpha-helical peptide and its double D-amino acid analog have been determined by means of 1H NMR and CD spectroscopies under equivalent conditions. The chemical shifts (NH and C alpha H) and the analysis of nuclear Overhauser effects show a split of the continuous helix for the all-L peptide into two helices at the position of double D-amino acid replacement. Hydrogen exchange rates correlate with water accessibilities in the hydrophobic/hydrophilic face and confirm the amphipathic helical structure in the all-L peptide as well as in its double D-amino acid analog. A significantly accelerated hydrogen isotope exchange rate is observed for the D-Ala9 backbone proton, implying an increased flexibility at that position. These results show that the incorporation of an adjacent pair of D-amino acids only causes a local change in structure and flexibility, which makes the double D replacement interesting as a tool for specific helix-disturbing modifications to search for helical conformations in biologically active peptides.