TY - JOUR
T1 - Peptide-induced formation of crystalline Sn 6O 4(OH) 4 nanoparticles under ambient conditions
AU - Matsuno, Hisao
AU - Kawashima, Yuki
AU - Serizawa, Takeshi
N1 - Copyright:
Copyright 2012 Elsevier B.V., All rights reserved.
PY - 2012
Y1 - 2012
N2 - The short peptides that specifically bind to SnO 2 nanoparticles (NPs) were selected by using a phage display method. After the fourth round selection, ten kinds of amino acid sequences were identified, and it was revealed that affinities of the obtained phages for SnO 2 NPs were relatively higher than that of the unselected library phages. The identified peptide sequences showed that amino acids having a hydroxy group and hydrophobic amino acids were enriched in the selection process. Binding constants (K a) of the chemically synthesized heptapeptides having the identified sequences were quantitatively estimated. The pTO-7 peptide (Ser-Ser-Ile-Leu-Arg- Phe-Pro) showed the greatest K a value (5.80 × 10 5 M -1 at 25°C) among the investigated peptides, and also showed binding specificity to SnO 2. The SnO 2-recognizing peptides functioned as nanostructure stabilizer during pH-dependent preparation of water-insoluble tin-based compound (Sn 6O 4(OH) 4) at room temperature. These effects as stabilizers to disperse nanostructures in water phase were greater than that of a general purpose stabilizer poly(vinylpyrrolidone). Dynamic light scattering and transmission electron microscope analyses revealed that the formed structures in the presence of the pTO-7 peptide were squarish NPs with an approximately 60 nm diameter, and wide-angle powder X-ray diffraction analyses suggested that its crystallinity was increased by existence of the peptide.
AB - The short peptides that specifically bind to SnO 2 nanoparticles (NPs) were selected by using a phage display method. After the fourth round selection, ten kinds of amino acid sequences were identified, and it was revealed that affinities of the obtained phages for SnO 2 NPs were relatively higher than that of the unselected library phages. The identified peptide sequences showed that amino acids having a hydroxy group and hydrophobic amino acids were enriched in the selection process. Binding constants (K a) of the chemically synthesized heptapeptides having the identified sequences were quantitatively estimated. The pTO-7 peptide (Ser-Ser-Ile-Leu-Arg- Phe-Pro) showed the greatest K a value (5.80 × 10 5 M -1 at 25°C) among the investigated peptides, and also showed binding specificity to SnO 2. The SnO 2-recognizing peptides functioned as nanostructure stabilizer during pH-dependent preparation of water-insoluble tin-based compound (Sn 6O 4(OH) 4) at room temperature. These effects as stabilizers to disperse nanostructures in water phase were greater than that of a general purpose stabilizer poly(vinylpyrrolidone). Dynamic light scattering and transmission electron microscope analyses revealed that the formed structures in the presence of the pTO-7 peptide were squarish NPs with an approximately 60 nm diameter, and wide-angle powder X-ray diffraction analyses suggested that its crystallinity was increased by existence of the peptide.
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U2 - 10.1246/bcsj.20120074
DO - 10.1246/bcsj.20120074
M3 - Article
AN - SCOPUS:84864261693
SN - 0009-2673
VL - 85
SP - 746
EP - 752
JO - Bulletin of the Chemical Society of Japan
JF - Bulletin of the Chemical Society of Japan
IS - 7
ER -