Charge of Phospholipids Determines the Rate of Lysozyme Aggregation but Not the Structure and Toxicity of Amyloid Aggregates.
Journal
The journal of physical chemistry letters
ISSN: 1948-7185
Titre abrégé: J Phys Chem Lett
Pays: United States
ID NLM: 101526034
Informations de publication
Date de publication:
29 Sep 2022
29 Sep 2022
Historique:
pubmed:
17
9
2022
medline:
1
10
2022
entrez:
16
9
2022
Statut:
ppublish
Résumé
Biophysical properties of plasma membranes are determined by a chemical structure of phospholipids, including saturation of fatty acids and charge of polar heads of these molecules. Phospholipids not only determine fluidity and plasticity of membranes but also play an important role in abrupt aggregation of misfolded proteins. In this study, we investigate the role of the charge of the most abundant phospholipids in the plasma membrane on the aggregation properties of the lysozyme. We found that the charge of phospholipids determines the aggregation rate of lysozyme and the morphology of the protein aggregates. However, the secondary structure and toxicity of these protein specimens are determined by the chemical nature rather than the charge of phospholipids. These findings show that the charge of phospholipids can be a key factor that determines the stability and aggregation mechanism of amyloidogenic proteins.
Identifiants
pubmed: 36111888
doi: 10.1021/acs.jpclett.2c02126
pmc: PMC10405293
mid: NIHMS1921606
doi:
Substances chimiques
Amyloid
0
Amyloidogenic Proteins
0
Fatty Acids
0
Phospholipids
0
Protein Aggregates
0
Muramidase
EC 3.2.1.17
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
8833-8839Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM142869
Pays : United States
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