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Shuguang Zhang. Dai, Jessica, 1981- Massachusetts Institute of Technology. Biological Engineering Division. Massachusetts Institute of Technology. Department of Biological Engineering 2005-06-02T19:45:38Z 2005-06-02T19:45:38Z 2004 2004 http://hdl.handle.net/1721.1/18046 57364247 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. 72 p. 2847381 bytes 2854875 bytes application/pdf application/pdf eng Massachusetts Institute of Technology MIT theses may be protected by copyright. Please reuse MIT thesis content according to the MIT Libraries Permissions Policy, which is available through the URL provided. http://dspace.mit.edu/handle/1721.1/7582 Biological Engineering Division. Characterization of self-assembling peptide nanofibers of KLD12 and RID 12 Thesis application/pdf false Publication unknown unknown <Publication xmlns="https://www.openaire.eu/cerif-profile/1.1/" id="f470a367-50e8-4537-bdb3-cadc1e2375c2"> <Type xmlns="https://www.openaire.eu/cerif-profile/vocab/COAR_Publication_Types">http://purl.org/coar/resource_type/c_1843</Type> <Language>eng</Language> <Title>Characterization of self-assembling peptide nanofibers of KLD12 and RID 12</Title> <PublishedIn> <Publication> </Publication> </PublishedIn> <PublicationDate>2004</PublicationDate> <Authors> <Author> <DisplayName>Dai, Jessica, 1981-</DisplayName> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> </Authors> <Editors> </Editors> <Publishers> <Publisher> <DisplayName>Massachusetts Institute of Technology</DisplayName> <OrgUnit /> </Publisher> </Publishers> <License>http://dspace.mit.edu/handle/1721.1/7582</License> <Keyword>Biological Engineering Division.</Keyword> <Abstract>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.</Abstract> <Access xmlns="http://purl.org/coar/access_right" > </Access> </Publication>