Saturation of fatty acids in phosphatidic acid uniquely alters transthyretin stability changing morphology and toxicity of amyloid fibrils.

Amyloid Fatty Acids Prealbumin Phosphatidic Acids Amyloidogenic Proteins
AFM-IR Fibrils Oligomers Phosphatidic acid Toxicity Transthyretin

Journal

Chemistry and physics of lipids
ISSN: 1873-2941
Titre abrégé: Chem Phys Lipids
Pays: Ireland
ID NLM: 0067206

Informations de publication

Date de publication:
Nov 2023
Historique:
received: 17 08 2023
revised: 11 10 2023
accepted: 15 10 2023
medline: 20 11 2023
pubmed: 20 10 2023
entrez: 20 10 2023
Statut: ppublish

Résumé

Transthyretin (TTR) is a small, β-sheet-rich tetrameric protein that transports thyroid hormone thyroxine and retinol. Phospholipids, including phosphatidic acid (PA), can uniquely alter the stability of amyloidogenic proteins. However, the role of PA in TTR aggregation remains unclear. In this study, we investigated the effect of saturation of fatty acids (FAs) in PA on the rate of TTR aggregation. We also reveal the extent to which PAs with different length and saturation of FAs altered the morphology and secondary structure of TTR aggregates. Our results showed that TTR aggregation in the equimolar presence of PAs with different length and saturation of FAs yielded structurally and morphologically different fibrils compared to those formed in the lipid-free environment. We also found that PAs drastically lowered the toxicity of TTR aggregates formed in the presence of this phospholipid. These results shed light on the role of PA in the stability of TTR and transthyretin amyloidosis.

Identifiants

DOI: 10.1016/j.chemphyslip.2023.105350 PMID: 37858615
pubmed: 37858615
pii: S0009-3084(23)00072-5
doi: 10.1016/j.chemphyslip.2023.105350
pii:
doi:

Substances chimiques

Amyloid 0
Fatty Acids 0
Prealbumin 0
Phosphatidic Acids 0
Amyloidogenic Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

105350

Informations de copyright

Copyright © 2023 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Abid Ali (A)

Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.

Kiryl Zhaliazka (K)

Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.

Tianyi Dou (T)

Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.

Aidan P Holman (AP)

Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States; Department of Entomology, Texas A&M University, College Station, TX 77843, United States.

Dmitry Kurouski (D)

Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States; Department of Biomedical Engineering, Texas A&M University, College Station, TX 77843, United States. Electronic address: dkurouski@tamu.edu.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Amyloïde › Saturation of fatty acids in phosphatidic acid...
questionsmedicales.fr › Lipides › Acides gras › Saturation of fatty acids in phosphatidic acid...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du sang › Sérumalbumine › Préalbumine › Saturation of fatty acids in phosphatidic acid...
questionsmedicales.fr › Lipides › Lipides membranaires › Phospholipides › Glycérophosphate › Acides phosphatidiques › Saturation of fatty acids in phosphatidic acid...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Amyloïde › Protéines amyloïdogènes › Saturation of fatty acids in phosphatidic acid...