Probing the interaction between peptides and metal oxides using point mutants of a TiO2-binding peptide

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 cons...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 24(2008), 13 vom: 01. Juni, Seite 6852-7
1. Verfasser: Chen, Haibin (VerfasserIn)
Weitere Verfasser: Su, Xiaodi, Neoh, Koon-Gee, Choe, Woo-Seok
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2008
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Metals Oxides Peptide Library titanium dioxide 15FIX9V2JP Titanium D1JT611TNE
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245 1 0 |a Probing the interaction between peptides and metal oxides using point mutants of a TiO2-binding peptide 
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520 |a 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 TiO2. 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 delta f or delta D 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 
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650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Oxides  |2 NLM 
650 7 |a Peptide Library  |2 NLM 
650 7 |a titanium dioxide  |2 NLM 
650 7 |a 15FIX9V2JP  |2 NLM 
650 7 |a Titanium  |2 NLM 
650 7 |a D1JT611TNE  |2 NLM 
700 1 |a Su, Xiaodi  |e verfasserin  |4 aut 
700 1 |a Neoh, Koon-Gee  |e verfasserin  |4 aut 
700 1 |a Choe, Woo-Seok  |e verfasserin  |4 aut 
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