Biotin-avidin interaction triggers conversion of triskelion peptide nanotori into nanochains

A biotinylated ditryptophan triskelion peptide molecule was synthesized and reported for its unique self assembly modulated by egg white protein, avidin. The presence of biotin over each arm of the synthesized triskelion peptide molecule supports its self assembly into a well defined robust nanotorus morphology in ethanol when deposited over a hydrophilic mica surface. Atomic force and electron microscopic techniques were used to investigate these nanotorus structures and the obtained results were further supported by spectroscopic investigations. Biotin-avidin interaction modules were applied to modulate these nanotorus structures to create other possible nanoarchitectures from this triskelion molecule. Interestingly, the dimerization of nanotorus structures was observed in the presence of avidin and appeared as the numbers 8 and 0. Furthermore, these nanotori simultaneously organized into an elongated random chain, which was appropriately aligned in a straight row when the solution of the nanotorus was spread over the avidin coated surface, thus providing an expeditious entry into creating interesting nanoarchitectures for potential nanotechnological applications.