ArticleScientific reports2017
Effects of Protein Corona on IAPP Amyloid Aggregation, Fibril Remodelling, and Cytotoxicity.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
23 citing papers in PubMed, 39 citations in OpenAlex.
- The protein corona at the nano-bio interface: the need for standardized methodology and opportunities for neurodegenerative disease intervention.RSC advances · 2026Review
- Effects of Liposome Composition and Size on Protein Corona Formation: Competitive Replacement of Abundant Proteins by High-Affinity Proteins on the Liposome Surface.Advanced healthcare materials · 2026Article
- Hydrodynamics and Aggregation of Nanoparticles with Protein Corona: Effects of Protein Concentration and Ionic Strength.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Determination of the Structure and Dynamics of the Fuzzy Coat of an Amyloid Fibril of IAPP Using Cryo-Electron Microscopy.Biochemistry · 2023Article
- Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases.Life (Basel, Switzerland) · 2023Review
- Correlation analysis between immune-related genes and cell infiltration revealed prostate cancer immunotherapy biomarkers linked to T cells gamma delta.Scientific reports · 2023Article
- Uncovering the universality of self-replication in protein aggregation and its link to disease.Science advances · 2022Article
- Nanoscale Surface Topography Modulates hIAPP Aggregation Pathways at Solid-Liquid Interfaces.International journal of molecular sciences · 2021Article
- Molecular Modeling of Protein Corona Formation and Its Interactions with Nanoparticles and Cell Membranes for Nanomedicine Applications.Pharmaceutics · 2021Review
- Amyloidosis Inhibition, a New Frontier of the Protein Corona.Nano today · 2020Article
- Human Plasma Protein Corona of Aβ Amyloid and Its Impact on Islet Amyloid Polypeptide Cross-Seeding.Biomacromolecules · 2020Article
- Heterotropic Modulation of Amylin Fibrillation by Small Molecules: Implications for Formulative Designs.The protein journal · 2020Article
- Morphological Determinants of Carbon Nanomaterial-Induced Amyloid Peptide Self-Assembly.Frontiers in chemistry · 2020Article
- Albumin Alters the Conformational Ensemble of Amyloid-β by Promiscuous Interactions: Implications for Amyloid Inhibition.Frontiers in molecular biosciences · 2020Article
- CaCOMaterials (Basel, Switzerland) · 2019Article
- Fatty Acids Compete with Aβ in Binding to Serum Albumin by Quenching Its Conformational Flexibility.Biophysical journal · 2019Article
- Physical and Toxicological Profiles of Human IAPP Amyloids and Plaques.Science bulletin · 2019Article
- Article
- Protein corona of airborne nanoscale PM2.5 induces aberrant proliferation of human lung fibroblasts based on a 3D organotypic culture.Scientific reports · 2018Article
- Star Polymers Reduce Islet Amyloid Polypeptide Toxicity via Accelerated Amyloid Aggregation.Biomacromolecules · 2017Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Aggregation of islet amyloid polypeptide (IAPP), a peptide hormone co-synthesized and co-stored with insulin in pancreatic cells and also co-secreted to the circulation, is associated with beta-cell death in type-2 diabetes (T2D). In T2D patients IAPP is found aggregating in the extracellular space of the islets of Langerhans. Although the physiological environments of these intra- and extra-cellular compartments and vascular systems significantly differ, the presence of proteins is ubiquitous but the effects of protein binding on IAPP aggregation are largely unknown. Here we examined the binding of freshly-dissolved IAPP as well as pre-formed fibrils with two homologous proteins, namely cationic lysozyme (Lys) and anionic alpha-lactalbumin (aLac), both of which can be found in the circulation. Biophysical characterizations and a cell viability assay revealed distinct effects of Lys and aLac on IAPP amyloid aggregation, fibril remodelling and cytotoxicity, pointing to the role of protein "corona" in conferring the biological impact of amyloidogenic peptides. Systematic molecular dynamics simulations further provided molecular and structural details for the observed differential effects of proteins on IAPP amyloidosis. This study facilitates our understanding of the fate and transformation of IAPP in vivo, which are expected to have consequential bearings on IAPP glycemic control and T2D pathology.
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