Unknown

Dataset Information

0

Biotin binders selected from a random peptide library expressed on phage.


ABSTRACT: Recombinant biotin-binding phages were affinity-selected from a random peptide library expressed on the surface of filamentous phage. Phage binding to biotinylated proteins was half-maximally inhibited by micromolar concentrations of a monobiotinylated molecule. Sequencing of the peptide inserts of selected phages led to the identification of a previously unknown biotin-binding motif, CXWXPPF(K or R)XXC. A synthetic peptide containing this sequence motif inhibited streptavidin binding to biotinylated BSA with an IC50 of 50 microM. This compound represents the shortest non-avidin biotin-binding peptide identified to date. Our results illustrate that phage display technology can be used to identify novel ligands for a small non-proteinaceous molecule.

SUBMITTER: Saggio I 

PROVIDER: S-EPMC1134410 | biostudies-other | 1993 Aug

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC4764921 | biostudies-literature
| S-EPMC2667759 | biostudies-literature
| S-EPMC6803038 | biostudies-literature
| S-EPMC3158561 | biostudies-literature
| S-EPMC3504085 | biostudies-literature
| S-EPMC4486725 | biostudies-literature
| S-EPMC5755776 | biostudies-literature
| S-EPMC2174457 | biostudies-other
| S-EPMC8999133 | biostudies-literature
| S-EPMC6437963 | biostudies-literature