Specificity and biomineralization activities of Ti-binding peptide-1 (TBP-1)
Specificity and biomineralization activities of Ti-binding peptide-1 (TBP-1)
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DOI：
10.1021/la047428m
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发表时间：
2005-03-29
期刊：
影响因子：
3.9
通讯作者：
Shiba, K
中科院分区：
文献类型：
--
作者：
Sano, KI;Sasaki, H;Shiba, K
许多识别无机材料的肽适体已经用体外肽进化系统分离出来。然而，目前尚不清楚肽是如何与无机材料相互作用的，以及这些相互作用的特异性如何。因此，我们通过监测肽适配体TBP-1 （RKLPDAPGMHTW）结合10种不同金属的能力来评估其靶特异性。我们发现噬菌体显示TBP-1与Ti、Si和Ag表面结合，而不是与Au、Cr、Pt、Sn、Zn、Cu或Fe表面结合。正如之前在Ti中看到的那样，R1A、P4A或D5A突变减少了TBP-1与Si和Ag的结合，这表明TBP-1与这三种材料结合的分子机制是相同的。我们还观察到合成的TBP-1肽介导了二氧化硅和银的矿化。因此，尽管Ti， Si和Ag表面的整体化学特征不同，但它们具有TBP-1识别的共同的热计量结构。
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 sulmanometric structure that is recognized by TBP-1.