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Peptides are particularly attrac- tive as molecular building blocks because their structural folding and stability have already been studied in detail [7– 9]. Self-assembling peptides have unique assembly charac- teristics that can be readily tuned by changing the amino acid sequence and conjugating chemical groups [2,10]. Their assembly mechanisms are governed by noncovalent inter- molecular interactions such as electrostatic, hydrophobic, van der Waals, hydrogen bonds and aromatic p-stacking [7]. Self-assembling peptides can adopt diverse 3D architec- tures such as vesicles, micelles, monolayers, bilayers, fibers, tubes, ribbons and tapes [11]. Furthermore, short peptides can be easily produced by standard chemical synthesis, avoiding the overall complexities of synthesizing large pro- teins [12]. They also provide necessary control over self- assembly based on physicochemical parameters such as pH, ionic strength, solvent, light and temperature [7,11]. Their biocompatibility makes them ideal candidates for stabiliz- ing labile components such as enzymes used in biosensors and bionanodevices
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