Magnetic Resonance Imaging Detects a Specific Peptide−Protein Binding Event
Luis M. De Leon Rodriguez(The University of Texas Southwestern Medical Center), Alfonso Bouzas Ortíz(Rogers (United States)), Allison L. Weiner(The University of Texas Southwestern Medical Center), Shanrong Zhang(The University of Texas Southwestern Medical Center), Zoltán Kovács(Rogers (United States)), Thomas Kodadek(Rogers (United States)), A. Dean Sherry(The University of Texas Southwestern Medical Center)
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Abstract
DOTA was conjugated to the N-terminus of a 12-mer peptide by using standard peptide synthesis chemistry. The peptide, first isolated by phage display, maintained a high affinity for its protein-binding target, Gal-80, even with GdDOTA attached. The high affinity constant (KA = 5 x 105 M-1) combined with the high relaxivity of the resulting GdDOTA-peptide.protein complex (r1bound = 44.8 +/- 1.7 mM-1 s-1) allowed detection of Gal-80 at muM levels using a standard magnetic resonance imaging protocol. This novel peptide-based, binding-activated MRI method could potentially be used to screen a wide variety of biomolecules.
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