Peptide aptamers: exchange of the thioredoxin-A scaffold by alternative platform proteins and its influence on target protein binding |
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Authors: | Klevenz B Butz K Hoppe-Seyler F |
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Institution: | (1) Angewandte Tumorvirologie, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, 69120 Heidelberg (Germany), Fax + 49 6221 424852, e-mail: hoppe-seyler@dkfz.de, DE |
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Abstract: | Peptide aptamers have emerged as powerful new tools for molecular medicine. They can specifically bind to and functionally
inactivate a given target molecule under intracellular conditions. Typically, peptide aptamers are generated by screening
a randomized peptide expression library, displayed from the Escherichia coli thioredoxin A (TrxA) protein. Here, we transferred peptide moieties from defined TrxA-based peptide aptamers to alternative
scaffold proteins, such as the green fluorescent protein and staphylococcal nuclease. Yeast and mammalian two-hybrid assays
as well as in vitro binding analyses show that the TrxA scaffold can be a major determinant for the binding of peptide aptamers.
In addition, we demonstrate that TrxA can correctly display peptide sequences that correspond to the binding domains of natural
interaction partners. Therefore, sequence analyses of TrxA-based peptide aptamers, isolated by two-hybrid screening from randomized
expression libraries, should also be useful to find cellular binding partners for a given target protein, by homology.
Received 1 August 2002; received after revision 17 September 2002; accepted 19 September 2002
RID="*"
ID="*"Corresponding author. |
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Keywords: | , Peptide aptamer, human papillomavirus, hepatitis B virus, protein scaffold, protein therapy, |
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