Mechanism underlying specificity of proteins targeting inorganic materials.
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 Ti-binding peptide.
Hayashi
Tomohiro
T
Department of Electronic Chemistry, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, Yokohama, Kanagawa 226-8502, Japan. tomo_hayashi@mac.com
Sano
Ken-Ichi
K
Shiba
Kiyotaka
K
Kumashiro
Yoshikazu
Y
Iwahori
Kenji
K
Yamashita
Ichiro
I
Hara
Masahiko
M
D000595:Amino Acid Sequence; D006046:Gold; D007287:Inorganic Chemicals / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012680:Sensitivity and Specificity; D055672:Static Electricity; D000267:Tissue Adhesions
D007287:Inorganic Chemicals; D011506:Proteins; D006046:Gold