Accession Number ADA582983
Title Biodiscovery of Aluminum Binding Peptides.
Publication Date Aug 2013
Media Count 18p
Personal Author A. S. Finch B. L. Adams D. Stratis-Cullum D. A. Sarkes M. M. Hurley
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.
Keywords Affinity reagent
Aluminum
Bacteria
Bacterial display
Bacteriophages
Binders
Biomineralization
Biosensing
Carbon nanotubes
Cells
Corrosion inhibition
Display systems
Escherichia coli
Expansion
Hybrid systems
Inorganic materials
Isolation
Membranes
Peptides
Proteins
Reprints
Solid binding peptides
Synthetic reagent
Toxins and antitoxins
Viruses
Yeasts


 
Source Agency Non Paid ADAS
NTIS Subject Category 57B - Biochemistry
Corporate Author Army Research Lab., Adelphi, MD.
Document Type Journal article
Title Note Conference paper.
NTIS Issue Number 1401
Contract Number N/A

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