Filamentous Phages Displaying Multivalent Peptide Motives With Specific Affinity To Anodic Alumina Surfaces
- *Corresponding Author:
- Joris Proost
Division of Materials and Process Engineering
Place Sainte-Barbe 2
Université catholique de Louvain
B-1348 Louvain-la-Neuve, Belgium
Tel: +32 10 47 93 42
Fax: +32 10 47 40 28
E-mail: [email protected]
Received Date: September 05, 2014; Accepted Date: December 10, 2014; Published Date: March 10, 2015
Citation: Proost J, Deschuyteneer G, Santoro R, Overmeere QV, Soumillion P, et al. (2015) Filamentous Phages Displaying Multivalent Peptide Motives with Specific Affinity to Anodic Alumina Surfaces. J Bioeng Biomed Sci 6:162. doi: 10.4172/2155-6210.1000162
Copyright: © 2015 Proost J, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
In this work, we report for the first time on the successful selection and identification of peptide motives that exhibit a specific affinity to anodic alumina surfaces when multivalently displayed on a filamentous phage. It was also demonstrated that, for a selected phage clone, a chemical functionalisation (biotinylation) of the bacteriophage does not deteriorate its specific affinity to anodic alumina. Moreover, such biotinylated bacteriophages, after being immobilised onto an anodic alumina surface, have been shown to allow for the quantitative detection of streptavidine using an ELISA protocol. These results are believed to pave the way for shifting the surface design of integrated biosensing devices from traditional, chemically modified synthetic surfaces, like silane-based self-assembled monolayers, towards molecular linkers based on genetically engineered polypeptides.