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| + | <span class="intro">The nowadays production methods of mAbs</span> are not only time-consuming and costly but are at the expense of animal lives. Antibodies have many applications in research, diagnostics, and show great promise in treatment of cancer. But the advancement is held back due to the expensive and tiresome production. Therefore we propose an alternative to antibodies; peptide aptamers – produced in Escherichia coli (<i>E. coli</i>). The variable loop of the peptide aptamer is generated through a random nucleotide library and held together by an enzymatic inactive version of human Thioredoxin (hTrx) as a scaffold protein. We are using the bacterial two-hybrid system to screen for functioning peptide aptamers that are able to bind our chosen target proteins (‘antigens’). In this model bacteria expressing a functioning peptide aptamer will express Red Fluorescent Protein (RFP), which enables us to isolate them. To challenge the antibody tradition, we are also proposing a production model. | ||
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Revision as of 17:17, 17 September 2015
"Change is the law of life and those who look only to the past or present are certain to miss the future." - John F. Kennedy
Project description
Monoclonal antibodies (mAbs) are extensively used in scientific and fundamental medical research. They are used to purify, detect and tag proteins, in diagnostics and treatments of diseases, just to mention some of the many purposes of mAbs. As schematized underneath, the production as it is, can be interpreted as consuming on multiple levels. We thought it was time for a skeptical approach, which is what our project is all about.
The nowadays production methods of mAbs are not only time-consuming and costly but are at the expense of animal lives. Antibodies have many applications in research, diagnostics, and show great promise in treatment of cancer. But the advancement is held back due to the expensive and tiresome production. Therefore we propose an alternative to antibodies; peptide aptamers – produced in Escherichia coli (E. coli). The variable loop of the peptide aptamer is generated through a random nucleotide library and held together by an enzymatic inactive version of human Thioredoxin (hTrx) as a scaffold protein. We are using the bacterial two-hybrid system to screen for functioning peptide aptamers that are able to bind our chosen target proteins (‘antigens’). In this model bacteria expressing a functioning peptide aptamer will express Red Fluorescent Protein (RFP), which enables us to isolate them. To challenge the antibody tradition, we are also proposing a production model.
Our team consists of nine students from five different educations; philosophy, chemical engineering, biochemistry and molecular biology, biomedicine and medicine. During this last 6 months we have laughed, cried, built friendships and overcome a lot of struggles together. In the end of the day it has just been a whole lot of fun! To guide and help us through the journey we have had our four supervisors. Go to next page the team and dig deeper into the members of the SDU 2015 team.