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Identifying Unique Material Binding Peptides Using a High Throughput Method

Krabacher, Rachel M.
http://orcid.org/0000-0001-7879-6174
http://rave.ohiolink.edu/etdc/view?acc_num=dayton1467888412

Abstract Details

2016, Master of Science (M.S.), University of Dayton, Chemical Engineering.
Through biotic-abiotic interactions, it has been shown that peptides can recognize and selectively bind to a wide variety of materials dependent on both their surface properties and the environment. Better understanding of these peptides and the materials to which they bind can be beneficial in the development of biofunctionalization approaches for creating hybrid materials and sensors. Several research groups have identified material binding peptides using biopanning with phage or cell peptide display libraries. However, limitations with sequence diversity of traditional bacteriophage (phage) display libraries and loss of unique phage clones during the amplification cycles results in a smaller pool of peptide sequences identified. In order to overcome some of the limitations of traditional biopanning methodology, a modified method using phage display along with high-throughput next generation sequencing to select for unique peptides specific for different classes of single wall carbon nanotubes has been devised. The process, analysis and characterization of peptide sequences identified using the modified method is described and compared to peptides identified using the traditional methods. Selected sequences from this study were immobilized on surfaces and used in site-specific capture of metallic and/or semiconducting carbon nanotubes. A dispersion experiment was carried out to identify chiral specific peptides. From this research, successful methods have been identified to select and confirm binding peptides specific to various materials. Knowledge of chiral specific recognizing peptides can allow for the potential purification and separation of specific chirality carbon nanotubes, thus opening the door for a number of carbon nanotube applications which had been previously hindered by mixed carbon nanotube samples.
Kristen Comfort, Dr. (Advisor)
Rajesh Naik, Dr. (Advisor)
Kevin Myers, Dr. (Committee Member)
Christina Harsch, Dr. (Committee Member)
210 p.
Biochemistry; Bioinformatics; Chemical Engineering; Materials Science
Carbon nanotubes; phage display; peptide immobilization; high throughput sequencing; bioinformatics; peptide binding; biotic-abiotic interaction

Recommended Citations

Citations

  • Krabacher, R. M. (2016). Identifying Unique Material Binding Peptides Using a High Throughput Method [Master's thesis, University of Dayton]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=dayton1467888412

    APA Style (7th edition)

  • Krabacher, Rachel. Identifying Unique Material Binding Peptides Using a High Throughput Method. 2016. University of Dayton, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=dayton1467888412.

    MLA Style (8th edition)

  • Krabacher, Rachel. "Identifying Unique Material Binding Peptides Using a High Throughput Method." Master's thesis, University of Dayton, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=dayton1467888412

    Chicago Manual of Style (17th edition)

dayton1467888412
552
© 2016, all rights reserved.
This open access ETD is published by University of Dayton and OhioLINK.
Release 3.2.12