Selection and mass spectrometry characterization of peptides targeting semiconductor surfaces

✍ Scribed by Elias Estephan; Christian Larroque; Nicole Bec; Pierre Martineau; Frédéric J.G. Cuisinier; Thierry Cloitre; Csilla Gergely

• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 616 KB
• Volume: 104
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.22478

✦ Synopsis

Abstract

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.