[HTML][HTML] EphB receptor-binding peptides identified by phage display enable design of an antagonist with ephrin-like affinity
M Koolpe, R Burgess, M Dail, EB Pasquale - Journal of Biological …, 2005 - ASBMB
The Eph receptor tyrosine kinases are overexpressed in many pathologic tissues and have
therefore emerged as promising drug target candidates. However, there are few molecules
available that can selectively bind to a single Eph receptor and not other members of this
large receptor family. Here we report the identification by phage display of peptides that bind
selectively to different receptors of the EphB class, including EphB1, EphB2, and EphB4.
Peptides with the same EphB receptor specificity compete with each other for binding …
therefore emerged as promising drug target candidates. However, there are few molecules
available that can selectively bind to a single Eph receptor and not other members of this
large receptor family. Here we report the identification by phage display of peptides that bind
selectively to different receptors of the EphB class, including EphB1, EphB2, and EphB4.
Peptides with the same EphB receptor specificity compete with each other for binding …