Magnetic resonance imaging detects a specific peptide-protein binding event

J Am Chem Soc. 2002 Apr 10;124(14):3514-5. doi: 10.1021/ja025511v.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Contrast Media / chemistry*
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism*
  • Heterocyclic Compounds / chemistry*
  • Magnetic Resonance Imaging / methods
  • Oligopeptides / chemistry
  • Oligopeptides / metabolism*
  • Organometallic Compounds / chemistry*
  • Protein Binding
  • Repressor Proteins*
  • Saccharomyces cerevisiae Proteins*

Substances

  • Contrast Media
  • Fungal Proteins
  • GAL80 protein, S cerevisiae
  • Heterocyclic Compounds
  • Oligopeptides
  • Organometallic Compounds
  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
  • gadolinium 1,4,7,10-tetraazacyclododecane-N,N',N'',N'''-tetraacetate