Biomolecular materials by design

The self-assembly of biological molecules for the design of novel materials with well-defined nanostructures is increasingly exploited in biotechnology. For instance, the designer peptide surfactants of the present contribution undergo self-assembly in water and form well-defined systems useful for various potential applications such as the encapsulation, the solubilization, or the crystallization of active biomolecules [1-3]. This family of amphiphilic peptides is intriguing because it consists of tuneable nanobiomaterials.

Current trend in nanotechnology is construction of nanostructured materials using the peptide-based self-assembly. These are key building blocks for future bio-nanotechnological applications. Importance of peptide as monomeric components is their capacity to be engineered to mediate spontaneous supramolecular self-assembly and their inherent chemical nature that facilitates chemical and biological recognition process.

Single enzyme studies have probed conformational fluctuations of enzymes and revealed an oscillating behavior [1-4] in their catalytic activity that remained masked in ensemble measurements. Various models have been proposed suggesting that the enzymes adopt a variety of interconverting conformations each one of them exhibiting different catalytic activity [3]. In most studies the enzymes are immobilized directly on a surface [4] on agarose gel [1], polystyrene beads [2], or even using proteins as foot [5].

We work on a new type of nanofabrication template composed of ordered high aspect ratio nanochannels in a chitin/protein composite material. Main components of the template are readily available from nature as part of the bristles of the marine worm aphrodita aculeata (class polychaeta, common name: sea mouse). The bristles of all polychaeta species are formed by secretion of chitin and protein at the base of cylindrical cell membrane extensions called microvilli.