Improved eIF4E binding peptides by phage display guided design: plasticity of interacting surfaces yield collective effects.

ABSTRACT: Eukaryotic initiation factor (eIF)4E is over-expressed in many types of cancer such as breast, head and neck, and lung. A consequence of increased levels of eIF4E is the preferential translation of pro-tumorigenic proteins (e.g. c-Myc and vascular endothelial growth factor) and as a result is regarded as a potential therapeutic target. In this work a novel phage display peptide has been isolated against eIF4E. From the phage sequence two amino acids were delineated which improved binding when substituted into the eIF4G1 sequence. Neither of these substitutions were involved in direct interactions with eIF4E and acted either via optimization of the helical capping motif or restricting the conformational flexibility of the peptide. In contrast, substitutions of the remaining phage derived am

SUBMITTER: Zhou W 

PROVIDER: S-EPMC3477164 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature