Abstract
A biotin-terminated nanofiber-formable oligopeptide (1), which consists of 16-mer hydrophobic Leu and hydrophilic Lys, was newly prepared in order to modificate nanofiber surface through antigen-antibody interaction. The secondary structure and self-assembling properties of 1 in water were evaluated by means of CD and AFM measurements. As a result, the peptide 1 was found to form relatively short nanofibers, compared to those from biotin-free peptide 2, with beta-sheet conformation in aqueous solution at pH 9. On the other hand, biotin-containing beta-sheet nanofibers with high-axial-ratio were successfully obtained by mixing the peptide 1 with 2. ·Fluorescence, AFM and TEM measurements clearly revealed that streptavidin interacted with the 1/2-nanofiber, and was immobilized on nanofiber · surface. These results demonstrate the potential of this nanofiber as novel biomaterials with a wide range of applications, such as nano-scaffold and nano-template.
