Studies from University of Strasbourg Have Provided New Information about Supramolecular Research (On the design of supramolecular assemblies made of peptides and lipid bilayers)
By a News Reporter-Staff News Editor at Life Science Weekly -- New research on Supramolecular Research is the subject of a report. According to news reporting originating in Strasbourg, France, by NewsRx journalists, research stated, "Peptides confer interesting properties to materials, supramolecular assemblies and to lipid membranes and are used in analytical devices or within delivery vehicles. Their relative ease of production combined with a high degree of versatility make them attractive candidates to design new such products."
The news reporters obtained a quote from the research from the University of Strasbourg, "Here, we review and demonstrate how CD- and solid-state NMR spectroscopic approaches can be used to follow the reconstitution of peptides into membranes and to describe some of their fundamental characteristics. Whereas CD spectroscopy is used to monitor secondary structure in different solvent systems and thereby aggregation properties of the highly hydrophobic domain of p24, a protein involved in vesicle trafficking, solid-state NMR spectroscopy was used to deduce structural information and the membrane topology of a variety of peptide sequences found in nature or designed. 15N chemical shift solid-state NMR spectroscopy indicates that the hydrophobic domain of p24 as well as a designed sequence of 19 hydrophobic amino acid residues adopt transmembrane alignments in phosphatidylcholine membranes. In contrast, the amphipathic antimicrobial peptide magainin 2 and the designed sequence LK15 align parallel to the bilayer surface. Additional angular information is obtained from deuterium solid-state NMR spectra of peptide sites labelled with 2H3-alanine, whereas 31P and 2H solid-state NMR spectra of the lipids furnish valuable information on the macroscopic order and phase properties of the lipid matrix. Using these approaches, peptides and reconstitution protocols can be elaborated in a rational manner, and the analysis of a great number of peptide sequences is reviewed."
According to the news reporters, the research concluded: "Finally, a number of polypeptides with membrane topologies that are sensitive to a variety of environmental conditions such as pH, lipid composition and peptide-to-lipid ratio will be presented."
For more information on this research see: On the design of supramolecular assemblies made of peptides and lipid bilayers. Journal of Peptide Science, 2014;20(7):526-536. Journal of Peptide Science can be contacted at: Wiley-Blackwell, 111 River St, Hoboken 07030-5774, NJ, USA. (Wiley-Blackwell - www.wiley.com/; Journal of Peptide Science - onlinelibrary.wiley.com/journal/10.1002/(ISSN)1099-1387)
Our news correspondents report that additional information may be obtained by contacting P.K. Koumkoua, Univ Strasbourg, CNRS, Inst Chim, UMR7177, F-67070 Strasbourg, France. Additional authors for this research include C. Aisenbrey, E. Salnikov, O. Rifi and B. Bechinger (see also Supramolecular Research).
Keywords for this news article include: France, Europe, Strasbourg, Nanotechnology, Emerging Technologies, Supramolecular Research, Supramolecular Assemblies
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