Identification of target-binding peptide motifs by high-throughput sequencing of phage-selected peptides.

ABSTRACT: High-throughput sequencing was previously applied to phage-selected peptides in order to gain insight into the abundance and diversity of isolated peptides. Herein we developed a procedure to efficiently compare the sequences of large numbers of phage-selected peptides for the purpose of identifying target-binding peptide motifs. We applied the procedure to analyze bicyclic peptides isolated against five different protein targets: sortase A, urokinase-type plasminogen activator, coagulation factor XII, plasma kallikrein and streptavidin. We optimized sequence data filters to reduce biases originating from the sequencing method and developed sequence correction algorithms to prevent identification of false consensus motifs. With our strategy, we were able to identify rare target-binding pep

SUBMITTER: Rentero Rebollo I 

PROVIDER: S-EPMC4267670 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature