Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation

Cell-surface sphingomyelin (SM) inhibits binary and ternary complex activity of blood coagulation by an unknown mechanism. Here we show the OH functionality of SM contributes in forming the close assembly through intermolecular H-bond and through Ca 2+ chelation, which restricts the protein-lipid/pr...

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Bibliographic Details
Published in:RSC advances 2021-01, Vol.11 (6), p.339-3398
Main Authors: Mallik, S, Prasad, R, Das, K, Sen, P
Format: Article
Language:English
Subjects:
Blood coagulation
Calcium ions
Chelation
Chemistry
Fatty acids
Lipids
NMR
Nuclear magnetic resonance
Proteins
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Summary:Cell-surface sphingomyelin (SM) inhibits binary and ternary complex activity of blood coagulation by an unknown mechanism. Here we show the OH functionality of SM contributes in forming the close assembly through intermolecular H-bond and through Ca 2+ chelation, which restricts the protein-lipid/protein-protein interactions and thus inhibits the coagulation procedure. Cell-surface sphingomyelin (SM) inhibits binary and ternary complex activity of blood coagulation.
ISSN:2046-2069
2046-2069
DOI:10.1039/d0ra09218e