Specificity and biomineralization activities of Ti-binding peptide-1 (TBP-1).
Numerous peptide aptamers that recognize inorganic materials have been isolated using in vitro peptide evolution systems. However, it remains unknown how peptides interact with inorganic materials or how specific those interactions are. We, therefore, assessed the target specificities of the peptide aptamer TBP-1 (RKLPDAPGMHTW) by monitoring its ability to bind 10 different metals. We found that phages displaying TBP-1 bound to Ti, Si, and Ag surfaces but not to Au, Cr, Pt, Sn, Zn, Cu, or Fe. As previously seen with Ti, binding to Si and Ag was diminished by R1A, P4A, or D5A mutation, suggesting that the same molecular mechanism underlies TBP-1 binding to all three materials. We also observed that a synthetic TBP-1 peptide mediated mineralization of both silica and Ag. It, thus, appears that although the overall chemical characteristics of Ti, Si, and Ag surfaces are dissimilar, they share a common subnanometric structure that is recognized by TBP-1.
Sano
Ken-Ichi
K
Department of Protein Engineering, Cancer Institute, Japanese Foundation for Cancer Research, 1-37-1 Kami-Ikebukuro, Toshima, Tokyo 170-8455, Japan.
Sasaki
Hiroyuki
H
Shiba
Kiyotaka
K
D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D046529:Microscopy, Electron, Transmission; D009154:Mutation / Q000235:genetics; D011485:Protein Binding; D012825:Silicon / Q000737:chemistry; D012834:Silver / Q000737:chemistry; D014025:Titanium / Q000737:chemistry* / Q000378:metabolism*
D002352:Carrier Proteins; D012834:Silver; D014025:Titanium; D012825:Silicon