Seminar Colour Guide:
External Faculty | External Postdoc | Company Representative Science and Society EMBL Distinguished Visitor Lecture Vision2020 Lecture Series Molecular Medicine Seminar | EIPOD Seminar | PSB Seminar | TAC Seminar Hamburg Speaker EMBL-La Sapienza Lecture
|Hamburg Speaker||Abstract: We synthesized a few sets of branched peptides constructed as 2-4 oligoglycine antennae jointed by their C-ends to an oligoamine core; length of the antennae is varied from one to ten glycine residues. The homologues with longer antennae are capable of spontaneous self-assembly (see the Figure), which is accompanied by formation of polyglycine II structure, both in aqueous solutions and at solid-water interfaces. Polyglycine II is non-canonical structure composed of parallel aligned peptide 31-helices, which are placed in points of a hexagonal lattice and bound together by hydrogen bonds. Morphologically the supramers formed are one molecule thick flat sheets/layers and, by the fact, should be considered as two-dimensional nanocrystals. |
Structures of self-assembling oligoglycines
Various nanoobjects (nanocrystal with optical, magnetic, or semiconducting properties, viruses, bacteria, natural or synthetic macromolecules) or relatively small functional molecules (biomolecules, photo- and chemosensors, etc.) may be immobilized (physically or chemically) on the surface of the described peptide nanocrystals and crystalline monolayers. Thus, we manage to cover the supramers facial surfaces with the trisaccharide Neu5Acá2-6Galâ1-4GlcNAcâ- (6'sialyllactosamine, 6'SLN) residues. This makes supramers being capable of tight binding with human influenza viruses thereby preventing contacts of the latter with target cells. High antiviral potency and absence signs of toxicity observed for the glycosupramers in vivo open prospects for their potential use as medication against flu.
|Hamburg Speaker||Abstract: tbd|