Measurement of fibrin concentration by fast field-cycling NMR.

Abstract:

:The relaxation of (1)H nuclei due to their interaction with quadrupolar (14)N nuclei in gel structures is measured using fast field-cycling NMR. This phenomenon called quadrupolar dips has been reported in different (1)H-(14)N bond-rich species. In this study, we have studied quadrupolar dips in fibrin, an insoluble protein that is the core matrix of thrombi. Fibrin was formed by the addition of thrombin to fibrinogen in 0.2% agarose gel. T(1)-dispersion curves were measured using fast field-cycling NMR relaxometry, over the field range of 1.5-3.5 MHz (proton Larmor frequency), and were analyzed using a curve-fitting algorithm. A linear increase of signal amplitude with increasing fibrin concentration was observed. This agrees with the current theory that predicts a linear relationship of signal amplitude with the concentration of contributing (14)N spins in the sample. Interestingly, fibrin formation gave rise to the signal, regardless of crosslinking induced by the transglutaminase factor XIIIa. To investigate the effect of proteins that might be trapped in the thrombi in vivo, the plasma protein albumin was added to the fibrin gel, and an increase in the quadrupolar signal amplitude was observed. This study can potentially be useful for thrombi classification by fast field-cycling MRI techniques.

journal_name

Magn Reson Med

authors

Broche LM,Ismail SR,Booth NA,Lurie DJ

doi

10.1002/mrm.23117

subject

Has Abstract

pub_date

2012-05-01 00:00:00

pages

1453-7

issue

5

eissn

0740-3194

issn

1522-2594

journal_volume

67

pub_type

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