Polyglycine II nanosheets: Supramolecular antivirals?
Tetraantennary peptides [glycinen-NHCH2]4C can form stable noncovalent structures by self-assembly through intermolecular hydrogen bonding. The oligopeptide chains assemble as polyglycine II to yield submicron-sized, flat, one-molecule-thick sheets. Attachment of α-N-acetylneuraminic acid (Neu5Acα) to the terminal glycine residues gives rise to water-soluble assembled glycopeptides that are able to bind influenza virus multivalently and inhibit adhesion of the virus to cells 103-fold more effectively than a monomeric glycoside of Neu5Acα. Another antiviral strategy based on virus-promoted assembly of the glycopeptides was also demonstrated. Consequently, the self-assembly principle offers new perspectives on the design of multivalent antivirals.