Albumin-Binding Domain Conjugate for Near-Infrared Fluorescence Lymphatic Imaging

Autor: Sunkuk Kwon, Cynthia Davies-Venn, Melissa B. Aldrich, Grace Wu, Barrett R. Harvey, Eva M. Sevick-Muraca, Pradip Ghosh, Bonnie Angermiller, Nathaniel Wilganowski
Jazyk: angličtina
Předmět:
Indocyanine Green
Cancer Research
Fluorescence-lifetime imaging microscopy
Fluorophore
Peptide
Plasma protein binding
Near-infrared fluorescence
03 medical and health sciences
chemistry.chemical_compound
Mice
0302 clinical medicine
Lymphatic imaging
Albumins
Medicine & Public Health
Albumin peptide conjugate
Animals
Humans
Radiology
Nuclear Medicine and imaging

030304 developmental biology
Fluorescent Dyes
Lymphatic Vessels
chemistry.chemical_classification
Medicine(all)
0303 health sciences
Binding Sites
Spectroscopy
Near-Infrared

Imaging / Radiology
Imaging agent
3. Good health
Transport protein
Mice
Inbred C57BL

Spectrometry
Fluorescence

Oncology
chemistry
Biochemistry
030220 oncology & carcinogenesis
Biophysics
Electrophoresis
Polyacrylamide Gel

Peptides
Binding domain
Conjugate
Research Article
Protein Binding
Zdroj: Molecular Imaging and Biology
ISSN: 1536-1632
DOI: 10.1007/s11307-011-0499-x
Popis: 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. Electronic supplementary material The online version of this article (doi:10.1007/s11307-011-0499-x) contains supplementary material, which is available to authorized users.
Databáze: OpenAIRE