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Title: Probing the interaction between peptides and metal oxides using point mutants of a TiO2-binding peptide
Authors: Chen, H.
Su, X.
Neoh, K.-G. 
Choe, W.-S. 
Issue Date: 1-Jul-2008
Citation: Chen, H., Su, X., Neoh, K.-G., Choe, W.-S. (2008-07-01). Probing the interaction between peptides and metal oxides using point mutants of a TiO2-binding peptide. Langmuir 24 (13) : 6852-6857. ScholarBank@NUS Repository.
Abstract: An increasing number of peptides with specific binding affinity to inorganic materials are being isolated using combinatorial peptide libraries without prior knowledge about the interaction between peptides and target materials. The lack of understanding of the mechanism and the contribution of constituent amino acids to the peptides' inorganic-binding ability poses an obstacle to optimizing and tuning of the binding affinity of peptides to inorganic materials and thus hinders the practical application of these peptides. Using the phage surface display technique, we previously identified a disulfide-bond-constrained peptide (-CHKKPSKSC-, STB1) cognitive of TiO 2. In the present study, the interaction of STB1 with TiO2 was probed using a series of point mutants of STB1 displayed on phage surfaces. Their binding affinity was measured using a quartz crystal microbalance with energy dissipation measurement and compared on the basis of the Δf or ΔD values. The three K residues of STB1 were found to be essential and sufficient for phage particle binding to TiO2. One mutant with five K residues showed not stronger but weaker binding affinity than STB1 due to its conformational restriction, as illustrated by molecular dynamics simulation, to align five K residues in a way conducive to their simultaneous interaction with the TiO2 surface. The contextual influence of noncharged residues on STB1's binding affinity was also investigated. Our results may provide insight into the electrostatic interaction between peptides and inorganic surfaces. © 2008 American Chemical Society.
Source Title: Langmuir
ISSN: 07437463
DOI: 10.1021/la800314p
Appears in Collections:Staff Publications

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