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...

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Bibliographic Details
Published in:Langmuir 2005-03, Vol.21 (7), p.3090-3095
Main Authors: Sano, Ken-Ichi, Sasaki, Hiroyuki, Shiba, Kiyotaka
Format: Article
Language:English
Subjects:
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - metabolism
Chemistry
Exact sciences and technology
General and physical chemistry
Microscopy, Electron, Transmission
Mutation - genetics
Protein Binding
Silicon - chemistry
Silver - chemistry
Titanium - chemistry
Titanium - metabolism
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Summary: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.
ISSN:0743-7463
1520-5827
DOI:10.1021/la047428m