Abstract：
: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-NH(2) 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 10.7microM, 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-NH(2) should prove useful for studies designed to evaluate N-cadherin function in various biological processes.
journal_name
Peptidesjournal_title
Peptidesauthors
Devemy E,Blaschuk OWdoi
10.1016/j.peptides.2008.06.025subject
Has Abstractpub_date
2008-11-01 00:00:00pages
1853-61issue
11eissn
0196-9781issn
1873-5169pii
S0196-9781(08)00283-0journal_volume
29pub_type
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