2010
DOI: 10.1016/j.biomaterials.2010.01.012
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Quantification of the binding affinity of a specific hydroxyapatite binding peptide

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Cited by 56 publications
(53 citation statements)
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“…Finally, colonies of infected E. coli cells are grown (each colony only multiplies one type of phage) and the amino-acid sequence of the binding peptides is deduced by evaluating the sequence of the phage DNA ( Figure 3). In material science, phage-display technology has been used for the selection of amino-acid sequences that bind specifically to various inorganic (GaAs (50), AlGaAs (50), valerite (51), calcite (52), hydroxyapatite) and polymeric materials (53)(54)(55)(56).…”
Section: Phage Display Assisted Design Of Bioconjugatesmentioning
confidence: 99%
“…Finally, colonies of infected E. coli cells are grown (each colony only multiplies one type of phage) and the amino-acid sequence of the binding peptides is deduced by evaluating the sequence of the phage DNA ( Figure 3). In material science, phage-display technology has been used for the selection of amino-acid sequences that bind specifically to various inorganic (GaAs (50), AlGaAs (50), valerite (51), calcite (52), hydroxyapatite) and polymeric materials (53)(54)(55)(56).…”
Section: Phage Display Assisted Design Of Bioconjugatesmentioning
confidence: 99%
“…Phage display was used to discover peptide sequences with selective affinity for HA [9093] or β-TCP [94]. In the latter study, a β-TCP binding domain was engineered onto EGF and the fusion protein was then anchored onto β-TCP disks.…”
Section: Functionalizing Bone-mimetic Scaffolds With Growth Factorsmentioning
confidence: 99%
“…In [43] it was found that phosphorylation (i.e., the introduction of C-site-binding groups) of a peptide had no effect on the affinity in case of chromatographic HA, but had a greater influence in the case of a more bone-like mineral. When phage display (i.e., a biological method to screen large libraries) was used to identify HAbinding linear peptides [4,44], several sequences, including STLPIPHEFSRE, VTKHLNQISQSY and SVSVGMKPSPRPGGGK emerged. In the last case, the SVSV fragment was mainly responsible for the interaction, whereas the MKPSP fragment apparently provided a conformational-dependent component that enhanced the peptide's binding, but by itself did not show any specific affinity.…”
Section: Interaction Mechanismsmentioning
confidence: 99%