Work

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

Year: 2013

Type: article

Abstract: 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).

Source: FEBS Letters

DOI: 10.1016/j.febslet.2013.10.017

Authors: Kosuke Tanegashima, Kohei Tsuji, Kenji Suzuki, Akira Shigenaga, Akira Otaka, Takahiko Hara

Institutions: Tokyo Metropolitan Institute of Medical Science, Tokushima University, Tokyo Medical and Dental University

Language: English

Topic: Chemokine receptors and signaling

Subfield: Oncology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: bronze

Funders: Mitsubishi Foundation, Japan Society for the Promotion of Science