Direct and Selective Immobilization of Proteins by Means of an Inorganic Material-Binding Peptide: Discussion on Functionalization in the Elongation to Material-Binding Peptide
Direct and Selective Immobilization of Proteins by Means of an Inorganic Material-Binding Peptide: Discussion on Functionalization in the Elongation to Material-Binding Peptide
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DOI：
10.1021/jp907731b
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发表时间：
2010-01-14
影响因子：
3.3
通讯作者：
Adschiri, Tadafumi
中科院分区：
文献类型：
--
作者：
Yokoo, Nozomi;Togashi, Takanari;Adschiri, Tadafumi
利用全人工肽库，我们已经确定了一个肽与ZnO材料的亲和力，可用于选择性地积累ZnO颗粒的聚丙烯-金板。在这项研究中，我们融合重组绿色荧光蛋白（GFP）与此氧化锌结合肽（ZnOBP），然后选择性地固定融合蛋白油氧化锌颗粒。我们确定了选择性固定重组GFP的所有适当条件，并通过将ZnOBP标签从单个氨基酸延长到完整序列来检查ZnOBP融合GFP的ZnO结合功能。ZnOBP与GFP的融合使得GFP油ZnO基质在适当的溶液中特异性吸附，并且热力学研究表明ZnOBP与ZnO表面之间的静电相互作用主要依赖于水蒸气。ZnO表面的ZnOBP的结合亲和力增加，首先在材料选择性方面，然后在高亲和力方面的GFP融合肽从一个单一的氨基酸延长到完整的ZnOBP。我们的结论是，ZnOBP和ZnO之间的相互作用依赖于水解的影响，不仅存在带电的氨基酸，但也在ZnOBP序列的周围残基。
Using all artificial peptide library, we have identified a peptide with affinity for ZnO materials that could be used to selectively accumulate ZnO particles oil polypropylene-gold plates. In this study, we fused recombinant green fluorescent protein (GFP) with this ZnO-binding peptide (ZnOBP) and then selectively immobilized the fused protein oil ZnO particles. We determined all appropriate condition for selective immobilization of recombinant GFP, and the ZnO-binding function of ZnOBP-fused GFP was examined by elongating the ZnOBP tag from a single amino acid to the intact sequence. The fusion of ZnOBP With GFP enabled specific adsorption of GFP oil ZnO Substrates in an appropriate Solution, and thermodynamic Studies showed a predominantly enthalpy-dependent electrostatic interaction between ZnOBP and the ZnO Surface. The ZnOBP's binding affinity for the ZnO Surface increased first ill terms of material selectivity and then in terms of high affinity as the GFP-fused peptide was elongated from a single amino acid to intact ZnOBP. We concluded that the enthalpy-dependent interaction between ZnOBP and ZnO was influenced by the presence of not only charged amino acids but also their surrounding residues in the ZnOBP sequence.