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The influence of zwitterionic and anionic phospholipids on protein aggregation.
Ali, Abid; Dou, Tianyi; Holman, Aidan P; Hung, Andrew; Osborne, Luke; Pickett, Davis; Rodriguez, Axell; Zhaliazka, Kiryl; Kurouski, Dmitry.
Afiliação
  • Ali A; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.
  • Dou T; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.
  • 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.
  • Hung A; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.
  • Osborne L; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.
  • Pickett D; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.
  • Rodriguez A; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.
  • Zhaliazka K; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, United States.
  • 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.
Biophys Chem ; 306: 107174, 2024 Mar.
Article em En | MEDLINE | ID: mdl-38211368
ABSTRACT
The progressive aggregation of misfolded proteins is the underlying molecular cause of numerous pathologies including Parkinson's disease and injection and transthyretin amyloidosis. A growing body of evidence indicates that protein deposits detected in organs and tissues of patients diagnosed with such pathologies contain fragments of lipid membranes. In vitro experiments also showed that lipid membranes could strongly change the aggregation rate of amyloidogenic proteins, as well as alter the secondary structure and toxicity of oligomers and fibrils formed in their presence. In this review, the effect of large unilamellar vesicles (LUVs) composed of zwitterionic and anionic phospholipids on the aggregation rate of insulin, lysozyme, transthyretin (TTR) and α- synuclein (α-syn) will be discussed. The manuscript will also critically review the most recent findings on the lipid-induced changes in the secondary structure of protein oligomers and fibrils, as well as reveal the extent to which lipids could alter the toxicity of protein aggregates formed in their presence.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Doença de Parkinson / Amiloidose Idioma: En Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Doença de Parkinson / Amiloidose Idioma: En Ano de publicação: 2024 Tipo de documento: Article