Year: 2006
Journal: Nanoletters., Vol. 6, No. 3, 2006, 515-519, 20100827
Authors: Hayashi T., Sano K-I., Shiba K., Kumashiro Y., Iwahori K., Yamashita I., Hara M.
Last authors: Masahiko Hara
Organizations: Department of Electronic Chemistry, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa 226-8502, Japan, Local Spatio-Temporal Functions aboratory, Frontier Research System, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan, Department of Protein Engineering, Cancer Institute, Japanese Foundation for Cancer research, and CREST, JST, 3-10-6 Ariake, Koto-ku, Tokyo 135-8550, Japan, Graduate School of Materials Science, Nara Institute of Science and Technology, and CREST, JST, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan, and AdVanced Technology Research Laboratories, Matsushita Electric Industrial Co., Ltd., 3-4 Hikari-dai, Seika, Kyoto 619-0237, Japan
Country: Japan
Adhesion force analysis using atomic force microscopy clearly revealed for the first time the mechanism underlying the specific binding between a titanium surface and ferritin possessing the sequence of Ti-binding peptide in its N-terminal domain. Our results proved that the specific binding is due to double electrostatic bonds between charged residue and surface groups of the substrate. Furthermore, it is also demonstrated that the accretion of surfactant reduces nonspecific interactions, dramatically enhancing the selectivity and specificity of Tibinding peptide.
