Journal
PEPTIDES
Volume 29, Issue 11, Pages 1853-1861Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2008.06.025
Keywords
N-cadherin antagonist; Peptide; Phage display; Endothelial cell
Funding
- Adherex Technologies
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The cell adhesion molecule, N-cadherin plays a pivotal role in many biological and disease processes. Drugs that modulate N-cadherin function should therefore be useful therapeutic agents. We have used phage display technology to identify amino acid sequences capable of binding to N-cadherin. All of these sequences harbor a Trp residue in the second position from the N-terminus. A synthetic linear peptide containing one of these sequences, H-SWTLYTPSGQSK-NH2 was found to bind a chimeric protein composed of the N-cadherin ectodomain fused to the immunoglobulin G1 Fc fragment with an affinity (K-D) of 10.7 mu M, as determined by surface plasmon resonance. It also blocked the aggregation of beads coated with this chimeric protein. Furthermore, this peptide disrupted adhesion and tube formation by N-cadherin-expressing human umbilical vein endothelial cells in vitro. These observations suggest that N-cadherin antagonists have the potential of serving as anti-angiogenic agents. The peptide, H-SWTLYTPSGQSK-NH2 should prove useful for studies designed to evaluate N-cadherin function in various biological processes. (C) 2008 Elsevier Inc. All rights reserved.
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