Novel (64)Cu- and (68)Ga-labeled RGD conjugates show improved PET imaging of α(ν)β(3) integrin expression and facile radiosynthesis

J Nucl Med. 2011 Aug;52(8):1276-84. doi: 10.2967/jnumed.111.087700. Epub 2011 Jul 15.

Abstract

PET with (18)F-labeled arginine-glycine-aspartic acid (RGD) peptides can visualize and quantify α(ν)β(3) integrin expression in patients, but radiolabeling is complex and image contrast is limited in some tumor types. The development of (68)Ga-RGD peptides would be of great utility given the convenience of (68)Ga production and radiolabeling, and (64)Cu-RGD peptides allow for delayed imaging with potentially improved tumor-to-background ratios.

Methods: We used the chelators DOTA,1,4,7-triazacyclononane,1-glutaric acid-4,7-acetic acid (NODAGA), and 4,11-bis(carboxymethyl)-1,4,8,11-tetraazabicyclo[6.6.2]hexadecane (CB-TE2A) to radiolabel the cyclic pentapeptide c(RGDfK) with (68)Ga or (64)Cu. NODAGA-c(RGDfK) was labeled at room temperature with both radionuclides within 10 min. Incubation at 95°C for up to 30 min was used for the other conjugates. The affinity profile of the metallopeptides was evaluated by a cell-based receptor-binding assay. Small-animal PET studies and biodistribution studies were performed in nude mice bearing subcutaneous U87MG glioblastoma xenografts.

Results: The conjugates were labeled with a radiochemical purity greater than 97% and specific activities of 15-20 GBq/μmol. The affinity profile was similar for all metallopeptides and comparable to the reference standard c(RGDfV). In the biodistribution studies, all compounds demonstrated a relatively similar tumor and normal organ uptake at 1 h after injection that was comparable to published data on (18)F-labeled RGD peptides. At 18 h after injection, however, (64)Cu-NODAGA-c(RGDfK) and (64)Cu-CB-TE2A-c(RGDfK) showed up to a 20-fold increase in tumor-to-organ ratios. PET studies demonstrated high-contrast images of the U87MG tumors at 18 h, confirming the biodistribution data.

Conclusion: The ease of radiolabeling makes (68)Ga-NODAGA-c(RGDfK) an attractive alternative to (18)F-labeled RGD peptides. The high tumor-to-background ratios of (64)Cu-NODAGA-c(RGDfK) and (64)Cu-CB-TE2A-c(RGDfK) at 18 h warrant testing of (64)Cu-labeled RGD peptides in patients.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding, Competitive
  • Cell Line, Tumor
  • Chelating Agents / pharmacology
  • Contrast Media / pharmacology
  • Copper Radioisotopes / pharmacology*
  • Female
  • Gallium Radioisotopes / pharmacology*
  • Gene Expression Regulation*
  • Humans
  • Integrin alphaVbeta3 / biosynthesis*
  • Mice
  • Mice, Nude
  • Neovascularization, Pathologic
  • Oligopeptides / chemistry*
  • Peptides / chemistry
  • Positron-Emission Tomography / methods*
  • Temperature
  • Time Factors

Substances

  • Chelating Agents
  • Contrast Media
  • Copper Radioisotopes
  • Gallium Radioisotopes
  • Integrin alphaVbeta3
  • Oligopeptides
  • Peptides
  • arginyl-glycyl-aspartic acid