C - Chemistry – Metallurgy – 07 – K
Patent
C - Chemistry, Metallurgy
07
K
C07K 14/52 (2006.01) A61K 38/08 (2006.01) A61K 38/17 (2006.01) A61K 38/19 (2006.01) C07K 7/06 (2006.01) C07K 14/715 (2006.01) C12Q 1/02 (2006.01) G01N 33/566 (2006.01) A61K 38/00 (2006.01)
Patent
CA 2226391
Peptides correspond ing to the N-terminal 9 residues of stromal cell derived factor-1 (SDF-1) have SDF-1 activity. Peptides, corresponding to residues 1-8, 1-9, and a disulfide linked dimer of 1-9, involving Cys-9, induced chemotaxis in T lymphocytes and CEM cells, and bound the SDF-1 receptor, CXC chemokine receptor 4 (CXCR4). The peptides had similar activities to SDF-1, but were less potent. Whereas native SDF-I had half maximal chemoattractant activity at 5 nM, the 1- 9 direr and a 1-9 monomer analog were 100- and 3600-fold less potent, respectively. Receptor desensitization and competition binding experiments indicated that the SDF-1 peptides are specific for CXCR4. As Cys-9 is involved in a disulfide bridge with Cys 34 in native SDF-1, it is possible that the disulfide of the peptide dimer enhances its structural similarity to the native protein. Overall this study shows that the N-terminal region is sufficient to bind and activate CXCR4, which suggests the feasibility of designing small CXCR4 agonists or antagonists.
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