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|Title:||QCM-D analysis of binding mechanism of phage particles displaying a constrained heptapeptide with specific affinity to SiO2 and TiO 2|
|Citation:||Chen, H., Su, X., Neoh, K.-G., Choe, W.-S. (2006-07-15). QCM-D analysis of binding mechanism of phage particles displaying a constrained heptapeptide with specific affinity to SiO2 and TiO 2. Analytical Chemistry 78 (14) : 4872-4879. ScholarBank@NUS Repository. https://doi.org/10.1021/ac0603025|
|Abstract:||A growing number of peptides capable of specifically recognizing inorganic materials have been reported, incrementally increasing the potential to harness peptides as a biological linker to bridge biomolecules and inorganic materials at nanometer scale. In this study, we identified disulfide bond constrained heptapeptides with specific binding affinity to SiO2 and TiO 2 using a phage display technique. Interestingly, two of the phage surface displayed peptides enriched with basic amino acid residues, STB1 (HKKPSKS) and STB2 (TKRNNKR), showed a cross binding affinity to both metal oxides. To understand the underlying binding mechanism, binding behaviors of phage particles harboring the STB1 (a high-frequency heptapeptide exhibiting dual binding affinity to both metal oxides) were investigated in a wide pH range using quartz crystal microbalance with energy dissipation measurement (QCM-D). It was found that the binding of STB1-harboring phages to the two metal oxides was clearly mediated by the peptide moiety displayed on the phage surface in a pH-dependent manner, indicating that the binding is largely governed by electrostatic interaction. Furthermore, the interpretation of QCM-D signals (i.e., frequency shift and dissipation shift), with the aid of AFM unage analysis of the phage particles bound on the surface of the two metal oxides, elucidated whether the nature of phage (or the displayed peptide) binding to the metal oxides is largely specific or nonspecific. © 2006 American Chemical Society.|
|Source Title:||Analytical Chemistry|
|Appears in Collections:||Staff Publications|
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