Biodiscovery of aluminum binding peptides

Bryn L. Adams; Deborah A. Sarkes; Amethist S. Finch; Margaret M. Hurley; Dimitra Stratis-Cullum

doi:10.1117/12.2015936

31 May 2013 Biodiscovery of aluminum binding peptides

Bryn L. Adams, Deborah A. Sarkes, Amethist S. Finch, Margaret M. Hurley, Dimitra Stratis-Cullum

Proceedings Volume 8719, Smart Biomedical and Physiological Sensor Technology X; 871909 (2013) https://doi.org/10.1117/12.2015936
Event: SPIE Defense, Security, and Sensing, 2013, Baltimore, Maryland, United States

Abstract

Cell surface peptide display systems are large and diverse libraries of peptides (7-15 amino acids) which are presented by a display scaffold hosted by a phage (virus), bacteria, or yeast cell. This allows the selfsustaining peptide libraries to be rapidly screened for high affinity binders to a given target of interest, and those binders quickly identified. Peptide display systems have traditionally been utilized in conjunction with organic-based targets, such as protein toxins or carbon nanotubes. However, this technology has been expanded for use with inorganic targets, such as metals, for biofabrication, hybrid material assembly and corrosion prevention. While most current peptide display systems employ viruses to host the display scaffold, we have recently shown that a bacterial host, Escherichia coli, displaying peptides in the ubiquitous, membrane protein scaffold eCPX can also provide specific peptide binders to an organic target. We have, for the first time, extended the use of this bacterial peptide display system for the biodiscovery of aluminum binding 15mer peptides. We will present the process of biopanning with macroscopic inorganic targets, binder enrichment, and binder isolation and discovery.

Citation Download Citation

Bryn L. Adams, Deborah A. Sarkes, Amethist S. Finch, Margaret M. Hurley, and Dimitra Stratis-Cullum "Biodiscovery of aluminum binding peptides", Proc. SPIE 8719, Smart Biomedical and Physiological Sensor Technology X, 871909 (31 May 2013); https://doi.org/10.1117/12.2015936

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