ArticlePrion
Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Amyloid fibrils of the myelin basic protein are an integral component of myelin in the vertebrate brain.Scientific reports · 2025Article
- Gene Therapy Approaches for Atherosclerosis Focusing on Targeting Lipid Metabolism and Inflammation.International journal of molecular sciences · 2025Review
- Yeast Glucan Remodeling Protein Bgl2p: Amyloid Properties and the Mode of Attachment in Cell Wall.International journal of molecular sciences · 2024Article
- Importance of Non-Covalent Interactions in Yeast Cell Wall Molecular Organization.International journal of molecular sciences · 2024Review
- Lipids and Lipoproteins in Atherosclerosis.Biomedicines · 2023Article
- Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response.Diseases (Basel, Switzerland) · 2023Review
- Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides.Nanomaterials (Basel, Switzerland) · 2021Article
- The Post-Translational Modifications, Localization, and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as a Key to Understanding their Functioning.International journal of molecular sciences · 2020Article
- Amyloidogenic Propensities of Ribosomal S1 Proteins: Bioinformatics Screening and Experimental Checking.International journal of molecular sciences · 2020Article
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019Review
- Screening for amyloid proteins in the yeast proteome.Current genetics · 2018Article
- Dataset of the molecular dynamics simulations of bilayers consisting of short amyloidogenic peptide VDSWNVLVAG from Bgl2p-glucantransferase ofData in brief · 2016Article
- Article
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Authors and funding
12 authors.
Funding
Abstract
The pH-dependence of the ability of Bgl2p to form fibrils was studied using synthetic peptides with potential amyloidogenic determinants (PADs) predicted in the Bgl2p sequence. Three PADs, FTIFVGV, SWNVLVA and NAFS, were selected on the basis of combination of computational algorithms. Peptides AEGFTIFVGV, VDSWNVLVAG and VMANAFSYWQ, containing these PADs, were synthesized. It was demonstrated that these peptides had an ability to fibrillate at pH values from 3.2 to 5.0. The PAD-containing peptides, except for VDSWNVLVAG, could fibrillate also at pH values from pH 5.0 to 7.6. We supposed that the ability of Bgl2p to form fibrils most likely depended on the coordination of fibrillation activity of the PAD-containing areas and Bgl2p could fibrillate at mild acid and neutral pH values and lose the ability to fibrillate with the increasing of pH values. It was demonstrated that Bgl2p was able to fibrillate at pH value 5.0, to form fibrils of various morphology at neutral pH values and lost the fibrillation ability at pH value 7.6. The results obtained allowed us to suggest a new simple approach for the isolation of Bgl2p from Saccharomyces cerevisiae cell wall.
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Registered trials
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