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Article Dans Une Revue Applied Surface Science Année : 2008

TOF-SIMS structural characterization of self-assembly monolayer of cytochrome b5 onto gold substrate.

Résumé

Orientation and three-dimensional structure of immobilized proteins on bio-devices are very important to assure their high performance. Time-of-flight secondary ion mass spectrometry (TOF-SIMS) is able to analyze upper surface of one layer of molecules. Orientation of immobilized proteins can be evaluated based on determination of a partial structure, representing ensemble of amino acids, on the surface part. In this study, a monolayer of cytochrome b5 was reconstituted onto gold substrate and investigated by surface plasmon resonance (SPR). After freeze-drying, the resulted protein self-assembly was evaluated using TOF-SIMS with the bismuth cluster ion source, and then TOF-SIMS spectra were analyzed to select peaks specific to cytochrome b5 and identify their chemical formula and ensembles of amino acids. The results from TOF-SIMS spectra analysis were compared to the amino acid sequence of the modified cytochrome b5 and three-dimensional structure of cytochrome b5 registered in the protein data bank. Finally, fragment-ion-generating parts of the immobilized-cytochrome b5 are determined based on the suggested residues and three-dimensional structure. These results suggest the actual structure and confirm the expected orientation of immobilized protein.
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Dates et versions

hal-00446995 , version 1 (13-01-2010)

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Satoka Aoyagi, Alain Rouleau, Wilfrid Boireau. TOF-SIMS structural characterization of self-assembly monolayer of cytochrome b5 onto gold substrate.. Applied Surface Science, 2008, 255, pp.1071-74. ⟨10.1016/j.apsusc.2008.05.086⟩. ⟨hal-00446995⟩
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