Mathematics

Studies from M.K. Baumann and co-researchers update current data on science

  2008 SEP 15 - (VerticalNews.com) -- According to a study from Zurich, Switzerland, "Small amphiphilic peptides are attractive building blocks to design biocompatible supramolecular structures via self-assembly, with applications in, for example, drug delivery, tissue engineering, and nanotemplating."

  "We address the influence of systematical changes in the amino acid sequence of such peptides on the self-assembled macromolecular structures. For cationic-head surfactant-like eight-residue peptides, the apolar tail amino acids were chosen to systematically vary the propensity to form an a-helical secondary structure while conserving the overall hydrophobicity of the sequence," wrote M.K. Baumann and colleagues.

  The researchers concluded: "Characterization of the supramolecular structures indicates that for short peptides a beta-sheetsecondary Structure correlates with ribbonlike assemblies while random-coil and a-helical secondary Structures correlate With assembly of rods."

  Baumann and colleagues published the results of their research in Langmuir (Understanding self-assembled amphiphilic peptide supramolecular structures from primary structure helix propensity. Langmuir, 2008;24(15):7645-7647).

  For additional information, contact E. Reimhult, Swiss Fed Institute Technology, Dept. of Materials Science, Surface Science & Technology Laboratory, Zurich, Switzerland.

  The publisher of the journal Langmuir can be contacted at: American Chemical Society, 1155 16th St., NW, Washington, DC 20036, USA.

  Keywords: Emerging Technologies, Engineering, Nanotech, Nanotechnology, Supramolecular, Supramolecular Structures, Tissue Engineering.

  This article was prepared by VerticalNews Mathematics editors from staff and other reports. Copyright 2008, VerticalNews Mathematics via VerticalNews.com.