ArticlePloS one2013
Macromolecular crowding as a suppressor of human IAPP fibril formation and cytotoxicity.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 70 citations in OpenAlex.
- Trial
- Impact of Stabilizing Osmolytes on the Conformational Dynamics of Human and Rat Islet Amyloid Polypeptides.Proteins · 2026Article
- Fine-Tuning hIAPP Amyloidogenesis: Probing Molecular Mechanisms via Fluorinated Core Substitutions.ACS bio & med chem Au · 2026Article
- Modulation of islet amyloid polypeptide induced β-cell toxicity and amyloid formation by serum albumin proteins.Biophysical chemistry · 2026Article
- Underestimated role of macromolecular crowding in bioengineeredMaterials today. Bio · 2025Article
- Accelerated amyloid fibril formation at the interface of liquid-liquid phase-separated droplets by depletion interactions.Protein science : a publication of the Protein Society · 2025Article
- Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis.Nature communications · 2022Article
- Protein Fibrillation under Crowded Conditions.Biomolecules · 2022Review
- Interaction of Human Resistin with Human Islet Amyloid Polypeptide at Charged Phospholipid Membranes.ACS omega · 2022Article
- Article
- Preparation of Asymmetric Vesicles with Trapped CsCl Avoids Osmotic Imbalance, Non-Physiological External Solutions, and Minimizes Leakage.Langmuir : the ACS journal of surfaces and colloids · 2021Article
- The kinetics of islet amyloid polypeptide phase-separated system and hydrogel formation are critically influenced by macromolecular crowding.The Biochemical journal · 2021Article
- Interaction of polyethylene glycol with cytochrome c investigated via in vitro and in silico approaches.Scientific reports · 2021Article
- Exploring the effects of cosolutes and crowding on the volumetric and kinetic profile of the conformational dynamics of a poly dA loop DNA hairpin: a single-molecule FRET study.Nucleic acids research · 2019Article
- hIAPP forms toxic oligomers in plasma.Chemical communications (Cambridge, England) · 2018Article
- Dual effect of PEG-PE micelle over the oligomerization and fibrillation of human islet amyloid polypeptide.Scientific reports · 2018Article
- Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus.Journal of diabetes research · 2016Review
- Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Journal of diabetes research · 2016Review
- The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPP.Journal of diabetes research · 2015Review
- What macromolecular crowding can do to a protein.International journal of molecular sciences · 2014Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biological cell is known to exhibit a highly crowded milieu, which significantly influences protein aggregation and association processes. As several cell degenerative diseases are related to the self-association and fibrillation of amyloidogenic peptides, understanding of the impact of macromolecular crowding on these processes is of high biomedical importance. It is further of particular relevance as most in vitro studies on amyloid aggregation have been performed in diluted solution which does not reflect the complexity of their cellular surrounding. The study presented here focuses on the self-association of the type-2 diabetes mellitus related human islet amyloid polypeptide (hIAPP) in various crowded environments including network-forming macromolecular crowding reagents and protein crowders. It was possible to identify two competing processes: a crowder concentration and type dependent stabilization of globular off-pathway species and a--consequently--retarded or even inhibited hIAPP fibrillation reaction. The cause of these crowding effects was revealed to be mainly excluded volume in the polymeric crowders, whereas non-specific interactions seem to be most dominant in protein crowded environments. Specific hIAPP cytotoxicity assays on pancreatic β-cells reveal non-toxicity for the stabilized globular species, in contrast to the high cytotoxicity imposed by the normal fibrillation pathway. From these findings it can be concluded that cellular crowding is able to effectively stabilize the monomeric conformation of hIAPP, hence enabling the conduction of its normal physiological function and prevent this highly amyloidogenic peptide from cytotoxic aggregation and fibrillation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.