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Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
supramolecular chemistry: synthesis of self-assembling peptides and glycopeptides

The interest to small molecule self-assembling is caused to high extent by the possibility to design nanomaterials with customized properties and molecular devices. The driving force of self-assembling is simultaneous formation of multiple hydrogen bonds between complementary fragments. Practically all such supramolecular ensembles described in literature are stable in non-polar organic solvents but not in water, water is unfavorable medium for hydrogen bonds. Indeed, only classic amphiphils as micelles and liposomes possess the ability to form non-covalent associates in water. Our goal was the design of non-covalent polymers, (Glycosyl-T)n where T fragment provides the assembling and carbohydrate part provides biological activity, soluble and stable in aqueous solution. We expected that such assemblies could display sharply increased activity due to multivalent interaction with carbohydrate-binding protein; the effect is well known for true glycopolymers. The main requirement to the T fragment was the lack of hydrophobic region, in order to avoid interaction with biological membranes, and maximal simplicity of structure. When synthesizing oligovalent glycopeptides, [glycinen-NHCH2]4C, we have observed that some of them possess the required properties, i.e. form assemblies (so-called tectomers) that are stable in aqueous solutions. Oligopeptide chains are joined in assemblies by polyglycine II type, forming water insoluble flat sheets of submicron size, one molecule thick (45 Å when n = 7). Reversible disassembling of tectomers takes place in concentrated solution of lithium bromide, trifluoroacetic acid, or upon heating. Due to rigidity, regulated thickness, NH2 functionality, and reversibility of self-assembly the obtained material is supposed to be prospective as atomically smooth platform for nanotechnology.
Neu5Ac-substituted tectomers bind influenza virus inhibiting its adhesion to receptor several orders of magnitude stronger than monomeric Neu5Ac glycoside. The self-assembly acts as amplifier of the ligand’s biological activity. Moreover, according to electron microscopy data, assembling of glycopeptides can be promoted by virion surface []. This approach gives new possibilities for a design of anti-adhesion therapeutics [] from cell-host (see ‘Inhibitors of influenza virus adhesion’).

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