Stability constants for Gd3+ binding to model DTPA‐conjugates and DTPA‐proteins: Implications for their use as magnetic resonance contrast agents

A. D. Sherry, W. P. Cacheris, Kuan Kah-Tiong Kuan

Research output: Contribution to journalArticle

118 Scopus citations

Abstract

Five DTPA‐amide and ester derivatives have been synthesized and their Gd3+ stability constants have been measured using a simple spectrophotometric method. These results are compared to stability constants measured for Gd3+ binding to two different DTPA‐conjugated proteins. Although the thermodynamic constants for Gd3+ binding to DTPA‐monopropylamide and DTPA‐monopropvlester relative to Gd( DTPA)2− decrease by log K = 2.6 and 3.4, respectively, the blood pH conditional constants differ from Gd( DTPA)2− only by log K = 1.2 and 1.9, respectively. The corresponding diprooylamide and ester conjugates of DTPA show considerably lower thermodynamic and conditional constants. This has important implications in the covalent attachment of chelates to macromolecules for use in magnetic resonance imaging. The measured binding constants for Gd(DTPA)‐IgG and Gd( DTPA)‐BSA suggest that many of the DTPA molecules in these systems, prepared under our experimental conditions, are diconjugated. The model compound results indicate that it is important to use methods in attaching DTPA to macromolecules which preclude diconjugation of the chelate. Otherwise, their affinity for Gd3+ and consequently their usefulness as MRI contrast agents may be severely compromised. © 1988 Academic Press, Inc.

Original languageEnglish (US)
Pages (from-to)180-190
Number of pages11
JournalMagnetic resonance in medicine
Volume8
Issue number2
DOIs
StatePublished - Oct 1988

ASJC Scopus subject areas

  • Radiology Nuclear Medicine and imaging

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