Dimeric peptides of the C-terminal region of CXCL14 function as CXCL12 inhibitors

作者：Tanegashima Kosuke; Tsuji Kohei; Suzuki Kenji; Shigenaga Akira; Otaka Akira; Hara Takahiko^*

来源：FEBS LETTERS, 2013, 587(23): 3770-3775.

DOI：10.1016/j.febslet.2013.10.017

• CXCL14
• CXCL12
• CXCR4
• alpha-Helix

We recently reported that CXCL14 binds to CXCR4 with high affinity and inhibits CXCL12-mediated chemotaxis. Here we found that the C-terminal 51-77 amino acid residues of CXCL14 are responsible for CXCR4 binding. A disulfide dimer peptide of CXCL14(51-77) bound to CXCR4 with comparable affinity to full length CXCL14, and exhibited CXCL12 inhibitor activity. CXCR4 was efficiently internalized upon binding of dimeric CXCL14(51-77), thereby being reduced on the cell surface. Substitution of 5 amino acid residues in combination with the use of an oxime linker for dimerization increased the solubility and chemical stability of the dimeric CXCL14(51-77). %26lt;br%26gt;Structured summary of protein interactions: %26lt;br%2

• 出版日期2013-11-29
• 单位河北医科大学