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iPEP: peptides designed and selected for interfering with protein interaction and function.

Mason, Jody M and Müller, Kristian M and Arndt, Katja M (2008) 'iPEP: peptides designed and selected for interfering with protein interaction and function.' Biochemical Society transactions, 36 (Pt 6). pp. 1442-7. ISSN 1470-8752

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Abstract

Semi-rational design is combined with PCAs (protein-fragment complementation assays) and phage-display screening techniques to generate a range of iPEPs (interfering peptides) that target therapeutically relevant proteins with much higher interaction stability than their native complexes. PCA selection has been improved to impose a competitive and negative design initiative on the library screen, thus simultaneously improving the specificity of assay 'winners'. The folding pathways of designed pairs imply that early events are dominated by hydrophobic collapse and helix formation, whereas later events account for the consolidation of more intricate intermolecular electrostatic interactions.

Item Type: Article
Uncontrolled Keywords: activator protein-1 (AP-1), basic leucine zipper (bZIP), interfering peptide, protein-fragment complementation assay (PCA), protein–protein interaction, semi-rational design.
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Biological Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 11 Oct 2011 10:39
Last Modified: 16 Dec 2014 11:21
URI: http://repository.essex.ac.uk/id/eprint/1069

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