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Peptide immobilisation on porous silicon surface for metal ions detection.

Sam SS, Chazalviel JN, Gouget-Laemmel AC, Ozanam FF, Etcheberry AA, Gabouze NE - Nanoscale Res Lett (2011)

Bottom Line: The recorded cyclic voltammograms show a quasi-irreversible process corresponding to the Cu(II)/Cu(I) couple.The kinetic factors (the heterogeneous rate constant and the transfer coefficient) and the stability constant of the complex formed on the porous silicon surface are determined.These results demonstrate the potential role of peptides grafted on porous silicon in developing strategies for simple and fast detection of metal ions in solution.

View Article: PubMed Central - HTML - PubMed

Affiliation: UDTS, 2 bd Frantz Fanon, BP 140, Alger-7 Merveilles, Algiers, Algeria. sabrina.sam@polytechnique.edu.

ABSTRACT
In this work, a Glycyl-Histidyl-Glycyl-Histidine (GlyHisGlyHis) peptide is covalently anchored to the porous silicon PSi surface using a multi-step reaction scheme compatible with the mild conditions required for preserving the probe activity. In a first step, alkene precursors are grafted onto the hydrogenated PSi surface using the hydrosilylation route, allowing for the formation of a carboxyl-terminated monolayer which is activated by reaction with N-hydroxysuccinimide in the presence of a peptide-coupling carbodiimide N-ethyl-N'-(3-dimethylaminopropyl)-carbodiimide and subsequently reacted with the amino linker of the peptide to form a covalent amide bond. Infrared spectroscopy (FT-IR) and X-ray photoelectron spectroscopy are used to investigate the different steps of functionalization.The property of peptides to form stable complexes with metal ions is exploited to achieve metal-ion recognition by the peptide-modified PSi-based biosensor. An electrochemical study of the GlyHisGlyHis-modified PSi electrode is achieved in the presence of copper ions. The recorded cyclic voltammograms show a quasi-irreversible process corresponding to the Cu(II)/Cu(I) couple. The kinetic factors (the heterogeneous rate constant and the transfer coefficient) and the stability constant of the complex formed on the porous silicon surface are determined. These results demonstrate the potential role of peptides grafted on porous silicon in developing strategies for simple and fast detection of metal ions in solution.

No MeSH data available.


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Transmission IR spectra of modified PSi. (a) Hydrogenated surface after electrochemical fabrication. (b) After thermal grafting of undecylenic acid. (c) After activation treatment of 90 min in an aqueous solution of 5 mM EDC and 5 mM NHS. (d) After amidation in 0.1 mM Gly-His-Gly-His in 1 × PBS buffer.
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Figure 1: Transmission IR spectra of modified PSi. (a) Hydrogenated surface after electrochemical fabrication. (b) After thermal grafting of undecylenic acid. (c) After activation treatment of 90 min in an aqueous solution of 5 mM EDC and 5 mM NHS. (d) After amidation in 0.1 mM Gly-His-Gly-His in 1 × PBS buffer.

Mentions: In the spectrum of the freshly prepared PSi layer (Figure 1a), one observes peaks characteristic of the SiH stretching modes, namely, the bands at 2,085 cm-1, 2,115 cm-1and 2,140 cm-1 ascribed to monohydride, dihydride and trihydride contributions, respectively [16]. The absence of any sizeable contribution in the 1,000-1,200 cm-1 range demonstrates that the PSi surface is oxide free [19]. The peak around 910 cm-1 corresponds to the deformation vibrations mode of Si-H2 (scissor deformation) [20]. After reaction with undecylenic acid (Figure 1b), the signature of acid chains grafted at the surface appears clearly. It consists of the contribution of the methylene backbone (symmetric and antisymmetric CH2 stretching mode at 2,855 and 2,925 cm-1, respectively, and CH2 scissor deformation mode at 1,465 cm-1), and that of the carboxyl groups (C=O stretching mode at 1,715 cm-1 and the C-O-H modes at 1,280 and 1,415 cm-1) [1,21]. After treatment of the obtained acid surface in EDC/NHS solution [22], a prominent triplet appears (Figure 1c) attesting the formation of a succimimidyl-ester termination. The main peak of this triplet at 1,740 cm-1 is ascribed to the antisymmetric stretching mode of the carbonyl groups of the succinimide cycle. The smaller peak at 1,785 cm-1 is ascribed to the corresponding symmetric mode, and that at 1,820 cm-1 is attributed to the ester C=O stretch [22,23]. Other characteristic bands of the terminal succinimidyl ester group include that with corresponding to the antisymmetric and symmetric stretching of the C-N-C group at 1,205 and 1,370 cm-1, and the C-O(-N) stretching vibration at 1,065 cm-1 [22,23]. After amidation (Figure 1d), the bands corresponding to the terminal succinimidyl ester group disappear and two broad characteristic bands are observed at 1,650 and 1,550 cm-1, commonly labelled amide I (νC=O) and amide II (δNH) [1,23]. The PSi surface remains essentially oxide free and the SiH stretching band intensities have decreased due to the partial substitution of the surface SiH species by the grafted chains.


Peptide immobilisation on porous silicon surface for metal ions detection.

Sam SS, Chazalviel JN, Gouget-Laemmel AC, Ozanam FF, Etcheberry AA, Gabouze NE - Nanoscale Res Lett (2011)

Transmission IR spectra of modified PSi. (a) Hydrogenated surface after electrochemical fabrication. (b) After thermal grafting of undecylenic acid. (c) After activation treatment of 90 min in an aqueous solution of 5 mM EDC and 5 mM NHS. (d) After amidation in 0.1 mM Gly-His-Gly-His in 1 × PBS buffer.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3211508&req=5

Figure 1: Transmission IR spectra of modified PSi. (a) Hydrogenated surface after electrochemical fabrication. (b) After thermal grafting of undecylenic acid. (c) After activation treatment of 90 min in an aqueous solution of 5 mM EDC and 5 mM NHS. (d) After amidation in 0.1 mM Gly-His-Gly-His in 1 × PBS buffer.
Mentions: In the spectrum of the freshly prepared PSi layer (Figure 1a), one observes peaks characteristic of the SiH stretching modes, namely, the bands at 2,085 cm-1, 2,115 cm-1and 2,140 cm-1 ascribed to monohydride, dihydride and trihydride contributions, respectively [16]. The absence of any sizeable contribution in the 1,000-1,200 cm-1 range demonstrates that the PSi surface is oxide free [19]. The peak around 910 cm-1 corresponds to the deformation vibrations mode of Si-H2 (scissor deformation) [20]. After reaction with undecylenic acid (Figure 1b), the signature of acid chains grafted at the surface appears clearly. It consists of the contribution of the methylene backbone (symmetric and antisymmetric CH2 stretching mode at 2,855 and 2,925 cm-1, respectively, and CH2 scissor deformation mode at 1,465 cm-1), and that of the carboxyl groups (C=O stretching mode at 1,715 cm-1 and the C-O-H modes at 1,280 and 1,415 cm-1) [1,21]. After treatment of the obtained acid surface in EDC/NHS solution [22], a prominent triplet appears (Figure 1c) attesting the formation of a succimimidyl-ester termination. The main peak of this triplet at 1,740 cm-1 is ascribed to the antisymmetric stretching mode of the carbonyl groups of the succinimide cycle. The smaller peak at 1,785 cm-1 is ascribed to the corresponding symmetric mode, and that at 1,820 cm-1 is attributed to the ester C=O stretch [22,23]. Other characteristic bands of the terminal succinimidyl ester group include that with corresponding to the antisymmetric and symmetric stretching of the C-N-C group at 1,205 and 1,370 cm-1, and the C-O(-N) stretching vibration at 1,065 cm-1 [22,23]. After amidation (Figure 1d), the bands corresponding to the terminal succinimidyl ester group disappear and two broad characteristic bands are observed at 1,650 and 1,550 cm-1, commonly labelled amide I (νC=O) and amide II (δNH) [1,23]. The PSi surface remains essentially oxide free and the SiH stretching band intensities have decreased due to the partial substitution of the surface SiH species by the grafted chains.

Bottom Line: The recorded cyclic voltammograms show a quasi-irreversible process corresponding to the Cu(II)/Cu(I) couple.The kinetic factors (the heterogeneous rate constant and the transfer coefficient) and the stability constant of the complex formed on the porous silicon surface are determined.These results demonstrate the potential role of peptides grafted on porous silicon in developing strategies for simple and fast detection of metal ions in solution.

View Article: PubMed Central - HTML - PubMed

Affiliation: UDTS, 2 bd Frantz Fanon, BP 140, Alger-7 Merveilles, Algiers, Algeria. sabrina.sam@polytechnique.edu.

ABSTRACT
In this work, a Glycyl-Histidyl-Glycyl-Histidine (GlyHisGlyHis) peptide is covalently anchored to the porous silicon PSi surface using a multi-step reaction scheme compatible with the mild conditions required for preserving the probe activity. In a first step, alkene precursors are grafted onto the hydrogenated PSi surface using the hydrosilylation route, allowing for the formation of a carboxyl-terminated monolayer which is activated by reaction with N-hydroxysuccinimide in the presence of a peptide-coupling carbodiimide N-ethyl-N'-(3-dimethylaminopropyl)-carbodiimide and subsequently reacted with the amino linker of the peptide to form a covalent amide bond. Infrared spectroscopy (FT-IR) and X-ray photoelectron spectroscopy are used to investigate the different steps of functionalization.The property of peptides to form stable complexes with metal ions is exploited to achieve metal-ion recognition by the peptide-modified PSi-based biosensor. An electrochemical study of the GlyHisGlyHis-modified PSi electrode is achieved in the presence of copper ions. The recorded cyclic voltammograms show a quasi-irreversible process corresponding to the Cu(II)/Cu(I) couple. The kinetic factors (the heterogeneous rate constant and the transfer coefficient) and the stability constant of the complex formed on the porous silicon surface are determined. These results demonstrate the potential role of peptides grafted on porous silicon in developing strategies for simple and fast detection of metal ions in solution.

No MeSH data available.


Related in: MedlinePlus