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001     916054
005     20230224084251.0
024 7 _ |a 10.3390/ijms232113185
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024 7 _ |a 1661-6596
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024 7 _ |a 2128/33515
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100 1 _ |a Sieme, Daniel
|0 0000-0001-9000-9938
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245 _ _ |a Metal Binding to Sodium Heparin Monitored by Quadrupolar NMR
260 _ _ |a Basel
|c 2022
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520 _ _ |a Heparins and heparan sulfate polysaccharides are negatively charged glycosaminoglycans and play important roles in cell-to-matrix and cell-to-cell signaling processes. Metal ion binding to heparins alters the conformation of heparins and influences their function. Various experimental techniques have been used to investigate metal ion-heparin interactions, frequently with inconsistent results. Exploiting the quadrupolar 23Na nucleus, we herein develop a 23Na NMR-based competition assay and monitor the binding of divalent Ca2+ and Mg2+ and trivalent Al3+ metal ions to sodium heparin and the consequent release of sodium ions from heparin. The 23Na spin relaxation rates and translational diffusion coefficients are utilized to quantify the metal ion-induced release of sodium ions from heparin. In the case of the Al3+ ion, the complementary approach of 27Al quadrupolar NMR is employed as a direct probe of ion binding to heparin. Our NMR results demonstrate at least two metal ion-binding sites with different affinities on heparin, potentially undergoing dynamic exchange. For the site with lower metal ion binding affinity, the order of Ca2+ > Mg2+ > Al3+ is obtained, in which even the weakly binding Al3+ ion is capable of displacing sodium ions from heparin. Overall, the multinuclear quadrupolar NMR approach employed here can monitor and quantify metal ion binding to heparin and capture different modes of metal ion-heparin binding.
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700 1 _ |a Griesinger, Christian
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700 1 _ |a Rezaie Ghaleh, Nasrollah
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773 _ _ |a 10.3390/ijms232113185
|g Vol. 23, no. 21, p. 13185 -
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856 4 _ |u https://juser.fz-juelich.de/record/916054/files/Metal%20Binding%20to%20Sodium%20Heparin%20Monitored%20by%20Quadrupolar%20NMR.pdf
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