[HTML][HTML] Albumin-binding domain conjugate for near-infrared fluorescence lymphatic imaging
CA Davies-Venn, B Angermiller, N Wilganowski… - Molecular imaging and …, 2012 - Springer
CA Davies-Venn, B Angermiller, N Wilganowski, P Ghosh, BR Harvey, G Wu, S Kwon…
Molecular imaging and biology, 2012•SpringerPurpose The aim of this study was to develop and characterize a novel peptide imaging
agent for noninvasive near-infrared fluorescence imaging of protein transport by the
lymphatics. An imaging agent consisting of a cyclic albumin-binding domain (cABD) peptide,
with sequence, Arg-Leu-Ile-Glu-Asp-Ile-Cys-Leu-Pro-Arg-Trp-Gly-Cys-Leu-Trp-Glu-Asp-Asp-
Lys, was conjugated to a near-infrared fluorophore, IRDye800CW, allowing for enhanced
vascular uptake, retention, and fluorescence imaging. Procedure Characterization of the …
agent for noninvasive near-infrared fluorescence imaging of protein transport by the
lymphatics. An imaging agent consisting of a cyclic albumin-binding domain (cABD) peptide,
with sequence, Arg-Leu-Ile-Glu-Asp-Ile-Cys-Leu-Pro-Arg-Trp-Gly-Cys-Leu-Trp-Glu-Asp-Asp-
Lys, was conjugated to a near-infrared fluorophore, IRDye800CW, allowing for enhanced
vascular uptake, retention, and fluorescence imaging. Procedure Characterization of the …
Purpose
The aim of this study was to develop and characterize a novel peptide imaging agent for noninvasive near-infrared fluorescence imaging of protein transport by the lymphatics. An imaging agent consisting of a cyclic albumin-binding domain (cABD) peptide, with sequence, Arg-Leu-Ile-Glu-Asp-Ile-Cys-Leu-Pro-Arg-Trp-Gly-Cys-Leu-Trp-Glu-Asp-Asp-Lys, was conjugated to a near-infrared fluorophore, IRDye800CW, allowing for enhanced vascular uptake, retention, and fluorescence imaging.
Procedure
Characterization of the cABD-IRDye800 peptide conjugate was performed using fluorescence spectroscopy to assess optical properties and SDS-PAGE and Biacore binding assays to determine binding affinity and specificity. Fluorescence imaging of normal C57BL/6 mice was conducted to monitor lymphatic uptake and retention.
Results
cABD-IRDye800 exhibited approximately six times greater fluorescent yield and greater stability than indocyanine green, an agent previously used in humans to image lymphatic vasculature. The agent exhibited affinity for albumin with IC50 and Kd in the nanomolar range and demonstrated superior retention characteristics within mouse lymphatics when compared with IRDye800CW.
Conclusions
cABD-IRDye800 has utility for assessing lymphatic function in mouse models of human lymphatic disease and the potential for use in clinical diagnostic imaging of the lymphatic vasculature.
Springer