Structure–activity relationship studies of a series of peptidomimetic ligands for α4 β1 integrin on Jurkat T-leukemia cells
✍ Scribed by Ruiwu Liu; Li Peng; Huijun Han; Kit S. Lam
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2006
- Tongue
- English
- Weight
- 357 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
α~4~β~1~ integrin is a therapeutic target for inflammation, autoimmune diseases, and lymphoid cancers. A series of peptidomimetic ligands based on the Nle‐D‐I motif have been synthesized and their binding affinities (IC~50~) to activated α~4~β~1~ integrin on Jurkat T‐leukemia cells have been determined using a cell adhesion assay. One of the 51 ligands, 18, has been determined to have an IC~50~ of 0.6 nM and has a more than twofold increase of binding affinity than the initial lead compound 1. Extensive SAR studies provide important information for further ligand optimization, which has served as a foundation for studies that ultimately led to identification of a potent ligand with an IC~50~ of 2 pM. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 595–604, 2006
This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]