ArticleThe journal of physical chemistry. B2013
Mutations and seeding of amylin fibril-like oligomers.
Article in The journal of physical chemistry. B, 2013. 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.
- Energetic profiling reveals thermodynamic principles underlying amyloid fibril maturation.Nature communications · 2025Article
- Analysis of Sheep and Goat IAPP Provides Insight into IAPP Amyloidogenicity and Cytotoxicity.Biochemistry · 2022Article
- d-Retro Inverso Amylin and the Stability of Amylin Fibrils.Journal of chemical theory and computation · 2020Article
- Effects of sedimentation, microgravity, hydrodynamic mixing and air-water interface on α-synuclein amyloid formation.Chemical science · 2020Article
- Stability of Aβ-fibril fragments in the presence of fatty acids.Protein science : a publication of the Protein Society · 2019Article
- Characterisation of the Structure and Oligomerisation of Islet Amyloid Polypeptides (IAPP): A Review of Molecular Dynamics Simulation Studies.Molecules (Basel, Switzerland) · 2018Review
- Mechanistic perspective and functional activity of insulin in amylin aggregation.Chemical science · 2018Article
- Amyloid β-Protein Assembly and Alzheimer's Disease: Dodecamers of Aβ42, but Not of Aβ40, Seed Fibril Formation.Journal of the American Chemical Society · 2016Article
- Inhibition of peptide aggregation by means of enzymatic phosphorylation.Beilstein journal of organic chemistry · 2016Article
- On the lack of polymorphism in Aβ-peptide aggregates derived from patient brains.Protein science : a publication of the Protein Society · 2015Article
- Causative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitus.Clinical interventions in aging · 2015Review
- On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides.Journal of diabetes research · 2015Review
- Stability of Iowa mutant and wild type Aβ-peptide aggregates.The Journal of chemical physics · 2014Article
- Article
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Authors and funding
3 authors.
Funding
Abstract
Seeding a protein solution with preformed fibrils can dramatically enhance the growth rate of amyloids. As the seeds do not need to be of the same protein, seeding may account for the observed correlations between amyloid diseases. In an effort to understand better the molecular mechanisms behind cross seeding we have studied in silico the effect of mutations on the seeding of amylin fibrils. Our investigations of the structural stability of decamers of wild type amylin peptides, of Y37L mutants, and of heteroassemblies of wild-type and mutant amylin molecules show that the experimentally observed efficient cross seeding can be explained based on similarity in fibril structure of components. We find that amyloids with similar side chains packing at the β-sheet interface are structurally compatible, acting as a good template for the congruent incorporation of homologues peptides. In the Y37L mutants, lack of tyrosine-specific interactions causes significant higher flexibility of the C terminal than observed in the wild-type fibril. This effects elongation of the mutant fibril leading to the longer lag times during aggregation that are observed in experiments. Our study gives guidelines for the design of ligands that could stabilize amylin fibrils.
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Registered trials
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