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Selection and mass spectrometry characterization of peptides targeting semiconductor surfaces
Author(s) -
Estephan Elias,
Larroque Christian,
Bec Nicole,
Martineau Pierre,
Cuisinier Frédéric J.G.,
Cloitre Thierry,
Gergely Csilla
Publication year - 2009
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.22478
Subject(s) - phage display , peptide , bacteriophage , mass spectrometry , adhesion , peptide library , chemistry , affinities , selection (genetic algorithm) , semiconductor , combinatorial chemistry , nanotechnology , materials science , chromatography , stereochemistry , biochemistry , optoelectronics , peptide sequence , escherichia coli , computer science , organic chemistry , artificial intelligence , gene
We report on elaboration of 12‐mer peptides that reveal specific recognition for the following semiconductor (SC) surfaces: GaAs(100), InAs(100), GaN(0001), ZnSe(100), ZnTe(100), GaAs(111)A, GaSb(100), CdSe(100). A M13 bacteriophage library was used to screen 10 9 different 12‐mer peptides against these substrates to finally isolate, in maximum six amplification cycles, peptides that bind to the target surfaces. The specific peptides for the InAs and ZnSe surfaces were obtained. Contrary, for the other SC surfaces several peptides with high affinities have been isolated. Aiming for a better specificity, when the phage display has been conducted through six cycles, the screening procedure got dominated by a phage present in the M13 bacteriophage library and the SVSVGMKPSPRP peptide has been selected for different SCs. The high amplification potential of this phage has been observed previously with different targets. Thus, precaution should be undertaken in defining adhesion peptides with the phage display technique and real affinity of the obtained biolinkers should be studied with other methods. We employed mass spectrometry (MALDI‐TOF/TOF) to demonstrate the preferential attachment (or not) of the SVSVGMKPSPRP peptide to the different SC surfaces. This allows us to define a realistic selection of the expressed peptides presenting affinity for the studied eight SC surfaces. We demonstrate that with increasing the dielectric constants of the employed solvents, adhesion of the SVSVGMKPSPRP peptide onto GaN(0001) is hindered. Biotechnol. Bioeng. 2009; 104: 1121–1131. © 2009 Wiley Periodicals, Inc.