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

doi:10.1021/ja025511v

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 journal › Article › peer-review

81 Scopus citations

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 (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.

Original language	English (US)
Pages (from-to)	3514-3515
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	124
Issue number	14
DOIs	https://doi.org/10.1021/ja025511v
State	Published - Apr 10 2002

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja025511v

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title = "Magnetic resonance imaging detects a specific peptide-protein binding event",

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 × 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.",

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AU - De León-Rodríguez, Luis M.

AU - Ortiz, Alfonso

AU - Weiner, Allison L.

AU - Zhang, Shanrong

AU - Kovacs, Zoltan

AU - Kodadek, Thomas

AU - Sherry, A. Dean

PY - 2002/4/10

Y1 - 2002/4/10

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AB - 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.

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Magnetic resonance imaging detects a specific peptide-protein binding event

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