Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

The vast potential applications of biomolecules that bind inorganic surfaces led mostly to the isolation of short peptides that target selectively specific materials. The demonstrated differential affinity toward certain surfaces created the impression that the recognition capacity of short peptides may match that of rigid biomolecules. In the following, we challenge this view by comparing the capacity of antibody molecules to discriminate between the (100) and (111A) facets of a gallium arsenide semiconductor crystal with the capacity of short peptides to do the same. Applying selection from several peptide and single chain phage display libraries, we find a number of antibody molecules that bind preferentially a given crystal facet but fail to isolate, in dozens of attempts, a single peptide capable of such recognition. The experiments underscore the importance of rigidity to the recognition of inorganic flat targets and therefore set limitations on potential applications of short peptides in biomimetics.

Type

Journal article

Journal

Journal of peptide science : an official publication of the European Peptide Society

Publication Date

06/2014

Volume

20

Pages

446 - 450

Addresses

Department of Biology, Technion - Israel Institute of Technology, Haifa, 32000, Israel; Department of Physics, Technion - Israel Institute of Technology, Haifa, 32000, Israel; The Russell Berrie Nanotechnology Institute, Technion - Israel Institute of Technology, Haifa, 32000, Israel.

Keywords

Arsenicals, Gallium, Oligopeptides, Antibodies, Enzyme-Linked Immunosorbent Assay, Surface Properties, Semiconductors