Selection process generating peptide aptamers and analysis of their binding to the TiO2 surface of a surface acoustic wave sensor

Gronewold, Thomas M. A.; Baumgartner, Antje; Weckmann, Andreas; Knekties, Jaqueline; Egler, Christian

doi:10.1016/j.actbio.2008.09.014

Cited by 20 publications

(29 citation statements)

References 16 publications

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“…In previous studies, SPR and QCM techniques were used to determine the kinetic off-rate constant of dissociation with peptides after adsorption on TiO 2 , SiO 2 , or hydroxyapatite surfaces. [49][50][51] However, results cannot be compared to those obtained in the present study because only peptides constituted with more than eight amino acids were used. In this study, the protocol used for peptide grafting into the AFM tip is expected to expose the carboxyl acid moiety (in the form of COO À at pH % 8) towards the SS surface.…”

Section: Afm Force Spectroscopy Of the D-ala-d-ala/ss Surface Interacmentioning

confidence: 81%

Probing Peptide–Inorganic Surface Interaction at the Single Molecule Level Using Force Spectroscopy

Landoulsi

Duprès

2011

ChemPhysChem

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We investigate the interaction between D-Ala-D-Ala peptide and a stainless steel (SS) surface by AFM force spectroscopy with view to understand the role and nature of interfacial processes at the single molecule level. For this purpose, force-distance curves were recorded between the D-Ala-D-Ala modified tip and the SS surface in NaHCO(3)-enriched medium. The SS surface was prepared in a way that allows iron oxide species, presumably FeOOH, to be formed and remains stable during AFM measurements. Dynamic force measurements show that the unbinding force linearly increases with the logarithm of the loading rate, as generally observed for receptor–ligand complexes. Our results reveal also the existence of two regimes, suggesting the presence of multiple energy barriers in the energy landscape. From these dynamic force spectroscopy measurements, the kinetic off-rate constant is determined. An average unbinding force in the range of 50-300 pN is obtained, depending on the loading rate. Accordingly, in a medium in which the electrostatic interactions are not dominating, the binding mechanism of the peptide and SS surface cannot be attributed to covalent bonds and may be due to a combination of van der Waals and hydrogen bonds. Our findings open up new way to probe peptide-inorganic surface interactions and to understand the mechanism of peptide specific binding which is of particular interest in the design of hybrid materials.

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Section: Afm Force Spectroscopy Of the D-ala-d-ala/ss Surface Interacmentioning

confidence: 81%

Probing Peptide–Inorganic Surface Interaction at the Single Molecule Level Using Force Spectroscopy

Landoulsi

Duprès

2011

ChemPhysChem

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“…Short peptide sequences interact with TiO 2 surface via electrostatic interaction also [57][58][59]. Yang et al [61] and Chen et al [62] stated that electrostatic interaction may be the main interaction between fibrinogen and TiO 2 surfaces.…”

Section: Adsorption Mechanism Of Rgdmentioning

confidence: 99%

“…Adsorption of protein on various materials has been widely studied and it has been found that factors such as electrostatic interaction, hydrophobic interaction, hydrogen bonding, VDW interaction and specific chemical interactions between protein and the adsorbent play important roles [56][57][58][59][60][61][62][63][64][65][66][67][68][69][70][71]. Short peptide sequences interact with TiO 2 surface via electrostatic interaction also [57][58][59].…”

Section: Adsorption Mechanism Of Rgdmentioning

confidence: 99%

Adsorption of tripeptide RGD on rutile TiO2 nanotopography surface in aqueous solution

et al. 2010

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“…Recent work by Gaebler et al [61] for calcium phosphate-based materials and by Micksch et al [19,62] for zirconia and different titanium alloys pioneered the application of this immobilization principle for the fixation of ODN on biomaterial relevant surfaces. In [19,62], eight peptide sequences were used based on a literature search for sequences binding to TiO 2 , SiO 2 , Ti6Al4V, and ZrO 2 [53][54][55]64,65]. The authors could show that AS 60mers linked to the substrate-binding peptide, sequences can be hybridized with biotinylated CS 31mers, with the statherin-derived peptide sequence giving the best results.…”

Section: Using Specific Substrate-binding Ligandsmentioning

confidence: 99%

Utilizing DNA for functionalization of biomaterial surfaces

2018

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DNA sequences are widely used for gene transfer into cells including a number of substrate surface-based supporting systems, but due to its singular structure property profile, DNA also offers multiple options for noncanonical applications. The special case of using DNA and oligodeoxyribonucleotide (ODN) structures for surface functionalization of biomedical implants is summarized here with the major focus on (a) immobilization or anchoring of nucleic acid structures on substrate surfaces, (b) incorporation of biologically active molecules (BAM) into such systems, and (c) biological characteristics of the resulting surfaces in vitro and in vivo. Sterilizations issues, important for potential clinical applications, are also considered.

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Selection process generating peptide aptamers and analysis of their binding to the TiO2 surface of a surface acoustic wave sensor

Cited by 20 publications

References 16 publications

Probing Peptide–Inorganic Surface Interaction at the Single Molecule Level Using Force Spectroscopy

Probing Peptide–Inorganic Surface Interaction at the Single Molecule Level Using Force Spectroscopy

Adsorption of tripeptide RGD on rutile TiO2 nanotopography surface in aqueous solution

Utilizing DNA for functionalization of biomaterial surfaces

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