Smith, Richard G.; Missailidis, Sotiris and Price, Michael R.
|DOI (Digital Object Identifier) Link:||http://doi.org/10.1016/S0378-4347(01)00422-4|
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A polyvalent, lytic phage display system (T7Select415-lb) displaying a random peptide library has been investigated for its ability to discover novel mimotopes reactive with the therapeutic monoclonal antibody C595. Sequence analysis of enriched phage lead to the identification of a predominant sequence RNREAPRGKICS, and two other consensus sequences RXXP and RXP. The novel synthetic peptide RNREAPRGKICS was linked to beaded agarose and the performance as a mimotope affinity chromatography matrix evaluated. Antibody purified using the novel matrix was found to be of higher specific reactivity than antibody purified using the conventional epitope matrix (peptide APDTRPAPG). The RNREAPRGKICS peptide binding to C595 demonstrated a higher equilibrium association constant (K-A=0.75 x 10(6)) than the epitope peptide (K-A=0.16 x 10(6)). Circular dichroism showed that the novel peptide had a more highly ordered structure at 4 degrees C and room temperature, than the epitope peptide.
|Item Type:||Journal Article|
|Extra Information:||Some of the symbols may not have transferred correctly into this bibliographic record and/or abstract.|
|Keywords:||affinity purification; polyvalent phage display library; anti-MUC1 antibodies; peptides; C595; bladder cancer|
|Academic Unit/Department:||Faculty of Science, Technology, Engineering and Mathematics (STEM) > Life, Health and Chemical Sciences
Faculty of Science, Technology, Engineering and Mathematics (STEM)
|Interdisciplinary Research Centre:||Biomedical Research Network (BRN)|
|Depositing User:||Sotiris Missailidis|
|Date Deposited:||05 Jul 2006|
|Last Modified:||04 Oct 2016 09:51|
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