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Biodiscovery of aluminum binding peptides / Bryn L. Adams [and four others].

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Format:
Book
Government document
Author/Creator:
Adams, Bryn L., author.
Contributor:
U.S. Army Research Laboratory, issuing body.
Language:
English
Subjects (All):
Peptides.
Peptides--Synthesis.
Synthetic biology.
Aluminum.
Biological reagents.
Biomineralization.
Synthetic Biology.
aluminum (metal).
Medical Subjects:
Synthetic Biology.
Aluminum.
Genre:
Text
Physical Description:
1 online resource (ii, 14 pages) : illustrations
Place of Publication:
Adelphi, MD : US Army Research Laboratory, 2013.
Language Note:
English
Summary:
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.
The original document contains color images. Reprint from Proceedings of SPIE v8719, 871909 p1-4, 2013
Notes:
"ARL-RP-0453."
"August 2013."
Offprint from: Proceedings of the SPIE, vol. 8719.
Includes bibliographical references (pages 10-12).
Approved for public release; distribution is unlimited.
text/html
Description based on online resource; title from PDF title page (DTIC website, viewed July 6, 2020).
OCLC:
872733820
Access Restriction:
Open access content Open access content

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