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/p...

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Detalles Bibliográficos
Autores principales: Mallik, S., Prasad, R., Das, K., Sen, P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2021
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8694017/
https://www.ncbi.nlm.nih.gov/pubmed/35424312
http://dx.doi.org/10.1039/d0ra09218e
Descripción
Sumario: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.

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