Phase-Dependent Adsorption of Myelin Basic Protein to Phosphatidylcholine Lipid Bilayers.
1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC)
lipid phase-dependent hydration of MBP hydrophobic amino acids
molecular dynamics (MD) simulations
myelin basic protein (MBP)
spectroscopic (UV-Vis, FTIR, CD) and calorimetric (DSC) measurements
Journal
Membranes
ISSN: 2077-0375
Titre abrégé: Membranes (Basel)
Pays: Switzerland
ID NLM: 101577807
Informations de publication
Date de publication:
04 Jan 2024
04 Jan 2024
Historique:
received:
24
11
2023
revised:
23
12
2023
accepted:
02
01
2024
medline:
22
1
2024
pubmed:
22
1
2024
entrez:
22
1
2024
Statut:
epublish
Résumé
The dense packing of opposite cytoplasmic surfaces of the lipid-enriched myelin membrane, responsible for the proper saltatory conduction of nerve impulses through axons, is ensured by the adhesive properties of myelin basic protein (MBP). Although preferentially interacting with negatively charged phosphatidylserine (PS) lipids, as an intrinsically disordered protein, it can easily adapt its shape to its immediate environment and thus adsorb to domains made of zwitterionic phosphatidylcholine (PC) lipids. As the molecular-level interaction pattern between MBP and PC lipid membranes suffers from scarce characterization, an experimental and computational study of multilamellar liposomes (MLVs) composed of 1,2-dipalmitoyl-
Identifiants
pubmed: 38248705
pii: membranes14010015
doi: 10.3390/membranes14010015
pii:
doi:
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : Croatian Science Foundation
ID : UIP-2020-02-7669