Date of Last Revision
2023-05-02 18:57:51
Major
Chemical Engineering - Cooperative Education
Degree Name
Bachelor of Science
Date of Expected Graduation
Spring 2016
Abstract
Protein modification shows promise for improving the effectiveness of protein therapy, including the use of Interferon-beta-1b for the treatment of multiple sclerosis. The addition of a chain of 50 lysine and glutamic acid residues (also called a KE50 modification) was tested on green fluorescent protein (AcGFP) to determine its effect on the bioactivity of the protein. Standard transformation protocol was used to grow the normal and modified proteins in E.Coli, and the bioactivity of the protein was measured using quantum yield and extinction coefficients to determine the reduction in brightness from the native form to the modified form. The brightness of the modified protein was reduced to 65% of the original brightness, showing that the modification reduces protein bioactivity but does not eliminate it. The same transformation experiment was attempted to grow native and KE50 modified versions of interferon-beta-1b, but the growth of the protein in E.Coli was not successful. If future efforts to create a modified version of interferon-beta-1b are successful, it could prove to be a more successful treatment for multiple sclerosis which has reduced immunogenicity and longer residence time in the blood compared to the current treatment.
Research Sponsor
Gang Cheng
First Reader
Lingyun Liu
Second Reader
Bi-min Zhang Newby
Recommended Citation
Burkey, Anna E., "Protein Sequence-Structure-Function Relationship: Testing KE-50 Modification on Recombinant Green Fluorescent Protein (AcGFP)" (2016). Williams Honors College, Honors Research Projects. 315.
https://ideaexchange.uakron.edu/honors_research_projects/315