Cargando…

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...

Descripción completa

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:
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
_version_ 1784619261698768896
author Mallik, S.
Prasad, R.
Das, K.
Sen, P.
author_facet Mallik, S.
Prasad, R.
Das, K.
Sen, P.
author_sort Mallik, S.
collection PubMed
description 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.
format Online
Article
Text
id pubmed-8694017
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher The Royal Society of Chemistry
record_format MEDLINE/PubMed
spelling pubmed-86940172022-04-13 Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation Mallik, S. Prasad, R. Das, K. Sen, P. RSC Adv Chemistry 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. The Royal Society of Chemistry 2021-01-15 /pmc/articles/PMC8694017/ /pubmed/35424312 http://dx.doi.org/10.1039/d0ra09218e Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Mallik, S.
Prasad, R.
Das, K.
Sen, P.
Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation
title Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation
title_full Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation
title_fullStr Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation
title_full_unstemmed Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation
title_short Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation
title_sort alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8694017/
https://www.ncbi.nlm.nih.gov/pubmed/35424312
http://dx.doi.org/10.1039/d0ra09218e
work_keys_str_mv AT malliks alcoholfunctionalityinthefattyacidbackboneofsphingomyelinguidestheinhibitionofbloodcoagulation
AT prasadr alcoholfunctionalityinthefattyacidbackboneofsphingomyelinguidestheinhibitionofbloodcoagulation
AT dask alcoholfunctionalityinthefattyacidbackboneofsphingomyelinguidestheinhibitionofbloodcoagulation
AT senp alcoholfunctionalityinthefattyacidbackboneofsphingomyelinguidestheinhibitionofbloodcoagulation