Magnetic resonance imaging detects a specific peptide-protein binding event

被引：70

作者：

De León-Rodríguez, LM

Ortiz, A

Weiner, AL

Zhang, SR

Kovacs, Z

Kodadek, T

Sherry, AD

机构：

[1] Univ Texas, SW Med Ctr, Ctr Biomed Invent, Dept Internal Med, Dallas, TX 75390 USA

[2] Univ Texas, SW Med Ctr, Ctr Biomed Invent, Dept Biol Mol, Dallas, TX 75390 USA

[3] Univ Texas, Dept Chem, Richardson, TX 75083 USA

[4] Rogers Magnet Resonance Ctr, Dept Radiol, Dallas, TX 75235 USA

[5] Macrocycl Inc, Dallas, TX 75252 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2002年 / 124卷 / 14期

关键词：

D O I：

10.1021/ja025511v

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. Copyright © 2002 American Chemical Society.

引用

页码：3514 / 3515

页数：2

共 12 条

[1] NMR EVIDENCE OF A LONG EXCHANGE LIFETIME FOR THE COORDINATED WATER IN LN(III)-BIS(METHYL AMIDE)-DTPA COMPLEXES (LN=GD, DY) [J].