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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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High-resolution XPS spectrum in the C1s region of GlyHisGlyHis-modified PSi.
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Figure 2: High-resolution XPS spectrum in the C1s region of GlyHisGlyHis-modified PSi.

Mentions: Figure 2 shows the C1s high-resolution XPS spectrum of the GlyHisGlyHis-modified PSi surface. This spectrum shows a peak centred at 285.4 eV with a fwhm of 1.4 eV and a weaker peak at 289 eV. The shoulders observed on either side of the main peak are indicative of the presence of carbon atoms in different environments. The signal can be deconvoluted into six peaks attributed to the different contributions of the carbon atoms. A tentative depiction of the types of carbon atoms that are distinguishable by XPS is shown in Figure 2. The weak peak at 284.5 eV is attributed to the carbon (shown as i) bonded to silicon. The CH2 moieties (shown as ii) in the alkyl chain are represented by two peaks. The first one at 285.2 eV is for the nearest carbon atoms from the PSi substrate and the second peak at 285.7 eV is for the carbon atoms close to the attached peptide [24]. The peak at 286.2 eV consists of the carbon atom of the alkyl chain (shown as iii) directly bonded to the peptide and the carbon atoms C=CH-N in the imidazole cycles [24,25]. The peak at 287 eV is ascribed to the carbon atoms (shown as iv) adjacent to amide functions and the carbon atoms (N=CH-N) in the imidazole cycles. Finally, the contribution at high binding energy (289 eV) is assigned to the acid and amide carbons (shown as v) [24,26].


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)

High-resolution XPS spectrum in the C1s region of GlyHisGlyHis-modified PSi.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 2: High-resolution XPS spectrum in the C1s region of GlyHisGlyHis-modified PSi.
Mentions: Figure 2 shows the C1s high-resolution XPS spectrum of the GlyHisGlyHis-modified PSi surface. This spectrum shows a peak centred at 285.4 eV with a fwhm of 1.4 eV and a weaker peak at 289 eV. The shoulders observed on either side of the main peak are indicative of the presence of carbon atoms in different environments. The signal can be deconvoluted into six peaks attributed to the different contributions of the carbon atoms. A tentative depiction of the types of carbon atoms that are distinguishable by XPS is shown in Figure 2. The weak peak at 284.5 eV is attributed to the carbon (shown as i) bonded to silicon. The CH2 moieties (shown as ii) in the alkyl chain are represented by two peaks. The first one at 285.2 eV is for the nearest carbon atoms from the PSi substrate and the second peak at 285.7 eV is for the carbon atoms close to the attached peptide [24]. The peak at 286.2 eV consists of the carbon atom of the alkyl chain (shown as iii) directly bonded to the peptide and the carbon atoms C=CH-N in the imidazole cycles [24,25]. The peak at 287 eV is ascribed to the carbon atoms (shown as iv) adjacent to amide functions and the carbon atoms (N=CH-N) in the imidazole cycles. Finally, the contribution at high binding energy (289 eV) is assigned to the acid and amide carbons (shown as v) [24,26].

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