A stable, high relaxivity, diaqua gadolinium complex that suppresses anion and protein binding

Dimitri Messeri; Mark P. Lowe; David Parker; Mauro Botta

doi:10.1039/b108294a

A stable, high relaxivity, diaqua gadolinium complex that suppresses anion and protein binding

Dimitri Messeri, Mark P. Lowe, David Parker, Mauro Botta

Department of Science and Technological Innovation

Research output: Contribution to journal › Article › peer-review

Abstract

The high relaxivity of [GdaDO3A]³⁻ (r_1p = 12.3 mM^-1 s^-1, 20 MHz, 298 K, τ_m = 30 ns) in water is maintained in serum solution because the binding of protein and endogeneous anions, e.g. HCO₃⁻/CO₃²⁻ is suppressed by electrostatic repulsion.

Original language	English
Pages (from-to)	2742-2743
Number of pages	2
Journal	Chemical Communications
Volume	1
Issue number	24
DOIs	https://doi.org/10.1039/b108294a
Publication status	Published - 2001

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10.1039/b108294a

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title = "A stable, high relaxivity, diaqua gadolinium complex that suppresses anion and protein binding",

abstract = "The high relaxivity of [GdaDO3A]3− (r1p = 12.3 mM-1 s-1, 20 MHz, 298 K, τm = 30 ns) in water is maintained in serum solution because the binding of protein and endogeneous anions, e.g. HCO3−/CO32− is suppressed by electrostatic repulsion.",

author = "Dimitri Messeri and Lowe, {Mark P.} and David Parker and Mauro Botta",

year = "2001",

doi = "10.1039/b108294a",

language = "English",

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journal = "Chemical Communications",

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publisher = "Royal Society of Chemistry",

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T1 - A stable, high relaxivity, diaqua gadolinium complex that suppresses anion and protein binding

AU - Messeri, Dimitri

AU - Lowe, Mark P.

AU - Parker, David

AU - Botta, Mauro

PY - 2001

Y1 - 2001

N2 - The high relaxivity of [GdaDO3A]3− (r1p = 12.3 mM-1 s-1, 20 MHz, 298 K, τm = 30 ns) in water is maintained in serum solution because the binding of protein and endogeneous anions, e.g. HCO3−/CO32− is suppressed by electrostatic repulsion.

AB - The high relaxivity of [GdaDO3A]3− (r1p = 12.3 mM-1 s-1, 20 MHz, 298 K, τm = 30 ns) in water is maintained in serum solution because the binding of protein and endogeneous anions, e.g. HCO3−/CO32− is suppressed by electrostatic repulsion.

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U2 - 10.1039/b108294a

DO - 10.1039/b108294a

M3 - Article

AN - SCOPUS:0035930740

SN - 1359-7345

VL - 1

SP - 2742

EP - 2743

JO - Chemical Communications

JF - Chemical Communications

IS - 24

ER -

A stable, high relaxivity, diaqua gadolinium complex that suppresses anion and protein binding

Abstract

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