Molecular substructure of the liquid-ordered phase formed by sphingomyelin and cholesterol: sphingomyelin clusters forming nano-subdomains are a characteristic feature.
Journal
Biophysical reviews
ISSN: 1867-2450
Titre abrégé: Biophys Rev
Pays: Germany
ID NLM: 101498573
Informations de publication
Date de publication:
Jun 2022
Jun 2022
Historique:
received:
11
05
2022
accepted:
26
05
2022
entrez:
6
7
2022
pubmed:
7
7
2022
medline:
7
7
2022
Statut:
epublish
Résumé
As a model of lipid rafts, the liquid-ordered (Lo) phase formed by sphingomyelin (SM) and cholesterol (Cho) in bilayer membranes has long attracted the attention of biophysics researchers. New approaches and methodologies have led to a better understanding of the molecular basis of the Lo domain structure. This review summarizes studies on model membrane systems consisting of SM/unsaturated phospholipid/Cho implying that the Lo phase contains SM-based nanodomains (or nano-subdomains). Some of the Lo phase properties may be attributed to these nanodomains. Several studies suggest that the nanodomains contain clustered SM molecules packed densely to form gel-phase-like subdomains of single-digit nanometer size at physiological temperatures. Cho and unsaturated lipids located in the Lo phase are likely to be concentrated at the boundaries between the subdomains. These subdomains are not readily detected in the Lo phase formed by saturated phosphatidylcholine (PC) molecules, suggesting that they are strongly stabilized by homophilic interactions specific to SM, e.g., between SM amide groups. This model for the Lo phase is supported by experiments using dihydro-SM, which is thought to have stronger homophilic interactions than SM, as well as by studies using the enantiomer of SM having opposite stereochemistry to SM at the 2 and 3 positions and by some molecular dynamics (MD) simulations of lipid bilayers containing Lo-lipids. Nanosized gel subdomains seem to play an important role in controlling membrane organization and function in biological membranes.
Identifiants
pubmed: 35791389
doi: 10.1007/s12551-022-00967-1
pii: 967
pmc: PMC9250586
doi:
Types de publication
Journal Article
Langues
eng
Pagination
655-678Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM122493
Pays : United States
Informations de copyright
© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2022.
Déclaration de conflit d'intérêts
Conflict of interestThe authors declare no competing interests.
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