Please use this identifier to cite or link to this item: https://doi.org/10.1021/ac0603025
DC FieldValue
dc.titleQCM-D analysis of binding mechanism of phage particles displaying a constrained heptapeptide with specific affinity to SiO2 and TiO 2
dc.contributor.authorChen, H.
dc.contributor.authorSu, X.
dc.contributor.authorNeoh, K.-G.
dc.contributor.authorChoe, W.-S.
dc.date.accessioned2014-10-09T06:59:47Z
dc.date.available2014-10-09T06:59:47Z
dc.date.issued2006-07-15
dc.identifier.citationChen, 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
dc.identifier.issn00032700
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/89966
dc.description.abstractA 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/ac0603025
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentCHEMICAL & BIOMOLECULAR ENGINEERING
dc.description.doi10.1021/ac0603025
dc.description.sourcetitleAnalytical Chemistry
dc.description.volume78
dc.description.issue14
dc.description.page4872-4879
dc.description.codenANCHA
dc.identifier.isiut000239017700015
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

89
checked on Aug 13, 2019

WEB OF SCIENCETM
Citations

91
checked on Aug 13, 2019

Page view(s)

95
checked on Aug 17, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.