Heteroditopic Binding of Magnetic Resonance Contrast Agents for Increased Relaxivity

被引：25

作者：

Zhang, Zhaoda ^{[1
]}

Kolodziej, Andrew F.

Greenfield, Matthew T.

Caravan, Peter ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Massachusetts Gen Hosp, AA Martinos Ctr Biomed Imaging, Charlestown, MA 02129 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2011年 / 50卷 / 11期

关键词：

fibrin; gadolinium; magnetic resonance imaging; peptides; rotational dynamics; MRI; THROMBUS; EP-2104R;

D O I：

10.1002/anie.201007689

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Kept within bounds: For peptide-targeted contrast agents, internal motion limits the relaxivity gain. A focused library approach identified an N-terminal thymine peptide nucleic acid (PNA) that reaches an additional binding pocket on the protein fibrin. The heteroditopic binding rigidifies the molecule upon binding, resulting in increased protein-bound relaxivity (see picture). Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：2621 / 2624

页数：4

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