Magnetic resonance imaging detects a specific peptide-protein binding event

Luis M. De León-Rodríguez, Alfonso Ortiz, Allison L. Weiner, Shanrong Zhang, Zoltan Kovacs, Thomas Kodadek, A. Dean Sherry

Research output: Contribution to journalArticlepeer-review

80 Scopus citations


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 × 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 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.

Original languageEnglish (US)
Pages (from-to)3514-3515
Number of pages2
JournalJournal of the American Chemical Society
Issue number14
StatePublished - Apr 10 2002

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


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