ArticleBiophysical journal2011
Resveratrol inhibits the formation of multiple-layered β-sheet oligomers of the human islet amyloid polypeptide segment 22-27.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Insight into the Neuroprotective Mechanisms of Resveratrol: Inhibition of Alpha-Synuclein Fibrillation and its Role in Mitigating Toxicity.Cell biochemistry and biophysics · 2026Article
- 3,4-Dihydroxybenzaldehyde Exerts Anti-Alzheimer's Effects by Inhibiting Aβ Protofibril Assembly and Activating Antioxidant Defense Mechanisms.International journal of molecular sciences · 2026Article
- Plant-Based Inhibitors of Protein Aggregation.Biomolecules · 2025Review
- Resveratrol protects pancreatic beta cell and hippocampal cells from the aggregate-prone capacity of hIAPP.Scientific reports · 2024Article
- Phosphorylated resveratrol as a protein aggregation suppressorRSC chemical biology · 2022Article
- Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes.Chemical reviews · 2021Review
- Mechanisms Underlying the Antidiabetic Activities of Polyphenolic Compounds: A Review.Frontiers in pharmacology · 2021Review
- Islet Amyloid Polypeptide: A Partner in Crime With Aβ in the Pathology of Alzheimer's Disease.Frontiers in molecular neuroscience · 2020Review
- Pre-structured hydrophobic peptide β-strands: A universal amyloid trap?Archives of biochemistry and biophysics · 2019Review
- Quantum chemical and molecular mechanics studies on the assessment of interactions between resveratrol and mutant SOD1 (G93A) protein.Journal of computer-aided molecular design · 2018Article
- Inhibition of protein misfolding and aggregation by natural phenolic compounds.Cellular and molecular life sciences : CMLS · 2018Review
- Amyloid-induced β-cell dysfunction and islet inflammation are ameliorated by 4-phenylbutyrate (PBA) treatment.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017Article
- Implications of peptide assemblies in amyloid diseases.Chemical Society reviews · 2017Review
- Unfolding Novel Mechanisms of Polyphenol Flavonoids for Better Glycaemic Control: Targeting Pancreatic Islet Amyloid Polypeptide (IAPP).Nutrients · 2017Review
- A Novel, Multi-Target Natural Drug Candidate, Matrine, Improves Cognitive Deficits in Alzheimer's Disease Transgenic Mice by Inhibiting Aβ Aggregation and Blocking the RAGE/Aβ Axis.Molecular neurobiology · 2017Article
- How accurate are your simulations? Effects of confined aqueous volume and AMBER FF99SB and CHARMM22/CMAP force field parameters on structural ensembles of intrinsically disordered proteins: Amyloid-βIntrinsically disordered proteins · 2017Article
- Stabilizing Off-pathway Oligomers by Polyphenol Nanoassemblies for IAPP Aggregation Inhibition.Scientific reports · 2016Article
- Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives.Journal of diabetes research · 2016Review
- Advanced protein formulations.Protein science : a publication of the Protein Society · 2015Review
- Alzheimer's disease--a panorama glimpse.International journal of molecular sciences · 2014Review
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The abnormal self-assembly of a number of proteins or peptides is a hallmark of >20 amyloidogenic diseases. Recent studies suggest that the pathology of amyloidogenesis can be attributed primarily to cytotoxic, soluble, intermediate oligomeric species rather than to mature amyloid fibrils. Despite the lack of available structural information regarding these transient species, many therapeutic efforts have focused on inhibiting the formation of these aggregates. One of the most successful approaches has been to use small molecules, many of which have been found to inhibit toxic species with high efficacy. A significant issue that remains to be resolved is the mechanism underlying the inhibitory effects of these molecules. In this article, we present extensive replica-exchange molecular dynamics simulations to study the early aggregation of the human islet amyloid polypeptide segment 22-27 in the presence and absence of the small-molecule inhibitor resveratrol. The simulations indicate that aggregation of these peptides was hindered by resveratrol via a mechanism of blocking the lateral growth of a single-layered β-sheet oligomer (rather than preventing growth by elongation along the fibril axis). Intersheet side-chain stacking, especially stacking of the aromatic rings, was blocked by the presence of resveratrol molecules, and the overall aggregation level was reduced.
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