Magnetic Resonance Imaging Detects a Specific Peptide−Protein Binding Event

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 (K A = 5 × 105 M-1) combined...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2002-04, Vol.124 (14), p.3514-3515
Main Authors: De León-Rodríguez, Luis M, Ortiz, Alfonso, Weiner, Allison L, Zhang, Shanrong, Kovacs, Zoltan, Kodadek, Thomas, Sherry, A. Dean
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biological and medical sciences
Contrast Media - chemistry
Fundamental and applied biological sciences. Psychology
Fungal Proteins - chemistry
Fungal Proteins - metabolism
Heterocyclic Compounds - chemistry
Interactions. Associations
Intermolecular phenomena
Magnetic Resonance Imaging - methods
Molecular biophysics
Oligopeptides - chemistry
Oligopeptides - metabolism
Organometallic Compounds - chemistry
Protein Binding
Repressor Proteins
Saccharomyces cerevisiae Proteins
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Summary: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 (K A = 5 × 105 M-1) combined with the high relaxivity of the resulting GdDOTA-peptide·protein complex (r 1bound = 44.8 ± 1.7 mM-1 s-1) allowed detection of Gal-80 at μM 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.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja025511v