C-terminal-modified LY2510924: a versatile scaffold for targeting C-X-C chemokine receptor type 4

Kentaro Suzuki1,2, Takashi Ui3, Akio Nagano4

  • 1RI Research Department, Research Division, FUJIFILM Toyama Chemical Co., Ltd., 453-1, Shimo-Okura, Matsuo-Machi, Sammu-City, Chiba, 289-1592, Japan. kentaro.a.suzuki@fujifilm.com.

Scientific Reports
|October 27, 2019
PubMed

Insights

A novel C-X-C chemokine receptor type 4 (CXCR4) antagonist, FRM001, shows specific binding and tumor accumulation. This modified LY2510924 derivative is a versatile scaffold for CXCR4-targeting probes in cancer imaging and therapy.

Area of Science:

  • Oncology
  • Radiochemistry
  • Molecular Imaging

Background:

  • C-X-C chemokine receptor type 4 (CXCR4) is a key target for cancer diagnosis and treatment.
  • LY2510924 is a known CXCR4 antagonist.

Purpose of the Study:

  • To evaluate a new 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid (DOTA)-conjugated CXCR4 antagonist, FRM001, derived from LY2510924.
  • To assess FRM001 and its metal complexes as CXCR4-targeting probes for tumor imaging and therapy.

Main Methods:

  • FRM001 synthesized by conjugating DOTA to LY2510924 via a cysteine linker.
  • CXCR4 binding affinity and metal complexation (Ga, Lu, Y) evaluated.
  • Cellular internalization and biodistribution studies in mice using 67Ga-FRM001.

Main Results:

  • FRM001 demonstrated CXCR4-specific binding with affinity comparable to LY2510924.
  • Binding affinity was maintained after complexation with Ga, Lu, and Y.
  • 67Ga-FRM001 showed high tumor and liver accumulation with rapid blood clearance in mice.
  • Hepatic accumulation was reduced by co-injecting AMD3100.

Conclusions:

  • C-terminal modification of LY2510924 yields FRM001, a versatile scaffold for developing CXCR4-targeting probes.
  • FRM001 and its metal complexes show potential for tumor imaging and therapy targeting CXCR4.