Thesis (M. Eng.)--Massachusetts Institute of Technology, Biological Engineering Division, 2004. / Includes bibliographical references (p. 70-72). / Self-assembling peptides are a promising new area of research with usage in numerous areas, from tissue engineering to membrane protein biology. This work is to further study the characteristics of the peptides KLD12 and RID12 and to generate new ways to control the properties of them. Peptide structures in solution were studied with circular dichroism and dynamic light scattering, and material properties of the peptide solutions were studied with rheology. Nanofiber structure was studied through atomic force microscopy. Sonication was found to have a minimal effect on KLD12, while pH could alter the length of the fibers formed. The presence of a second type of peptide in solution interacted with nanofibers of another peptide and resulted in a decrease of average fiber length. Peptide solutions transitioned from a viscous solution to a gel as the concentration of peptide increased, both alone and in mixture with another peptide. Understanding the properties of these peptides will help researchers design new biomaterials and improve applications of self-assembling peptides. / by Jessica Dai. / M.Eng.
| Identifer | oai:union.ndltd.org:MIT/oai:dspace.mit.edu:1721.1/18046 |
| Date | January 2004 |
| Creators | Dai, Jessica, 1981- |
| Contributors | Shuguang Zhang., Massachusetts Institute of Technology. Biological Engineering Division., Massachusetts Institute of Technology. Biological Engineering Division. |
| Publisher | Massachusetts Institute of Technology |
| Source Sets | M.I.T. Theses and Dissertation |
| Language | English |
| Detected Language | English |
| Type | Thesis |
| Format | 72 p., 2847381 bytes, 2854875 bytes, application/pdf, application/pdf, application/pdf |
| Rights | MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission., http://dspace.mit.edu/handle/1721.1/7582 |
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