ArticlePhysical chemistry chemical physics : PCCP2017
Oligomerization of FVFLM peptides and their ability to inhibit beta amyloid peptides aggregation: consideration as a possible model.
Article in Physical chemistry chemical physics : PCCP, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 41 citations in OpenAlex.
- Preeclampsia as a reversible risk factor for Alzheimer's disease: A prospective MRI study on morphological changes of the cerebral cortex and impairment of cognitive functions.The journal of prevention of Alzheimer's disease · 2026Article
- The association between mean arterial pressure and memory decline in preeclampsia patients: a mediation analysis of serum amyloid-β 1-42 and phosphorylated tau 181.BMC pregnancy and childbirth · 2025Article
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- AβJournal of molecular histology · 2024Article
- Protein Misfolding in Pregnancy: Current Insights, Potential Mechanisms, and Implications for the Pathogenesis of Preeclampsia.Molecules (Basel, Switzerland) · 2024Review
- The interaction of peptide inhibitors and Aβ protein: Binding mode analysis, inhibition of the formation of Aβ aggregates, and then exert neuroprotective effects.Frontiers in aging neuroscience · 2023Article
- Discovering new peripheral plasma biomarkers to identify cognitive decline in type 2 diabetes.Frontiers in cell and developmental biology · 2022Article
- Small Peptides for Inhibiting Serum Amyloid A Aggregation.ACS medicinal chemistry letters · 2021Article
- Identification of Patients with Preeclampsia by Measuring Fluorescence of an Amyloid-Binding Aryl Cyano Amide in Human Urine Samples.Analytical chemistry · 2018Article
- Role of Resultant Dipole Moment in Mechanical Dissociation of Biological Complexes.Molecules (Basel, Switzerland) · 2018Article
- Kinetics and mechanical stability of the fibril state control fibril formation time of polypeptide chains: A computational study.The Journal of chemical physics · 2018Article
- Mutations Alter RNA-Mediated Conversion of Human Prions.ACS omega · 2018Article
- Out-of-Register AβJournal of chemical theory and computation · 2018Article
- Conversion between parallel and antiparallel β-sheets in wild-type and Iowa mutant AβThe Journal of chemical physics · 2018Article
- Molecular dynamics simulations of early steps in RNA-mediated conversion of prions.Protein science : a publication of the Protein Society · 2017Article
- Immunological Tolerance, Pregnancy, and Preeclampsia: The Roles of Semen Microbes and the Father.Frontiers in medicine · 2017Article
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
Preeclampsia, a pregnancy-specific disorder, shares typical pathophysiological features with protein misfolding disorders including Alzheimer's disease. Characteristic for preeclampsia is the involvement of multiple proteins of which fragments of SERPINA1 and β-amyloid co-aggregate in urine and placenta of preeclamptic women. To explore the biophysical basis of this interaction, we investigated the multidimensional efficacy of the FVFLM sequence in SERPINA1, as a model inhibitory agent of β-amyloid aggregation. After studying the oligomerization of FVFLM peptides using all-atom molecular dynamics simulations with the GROMOS43a1 force field and explicit water, we report that FVFLM can aggregate and its aggregation is spontaneous with a remarkably faster rate than that recorded for KLVFF (aggregation "hot-spot" from β-amyloid). The fast kinetics of FVFLM aggregation was found to be driven primarily by core-like aromatic interactions originating from the anti-parallel orientation of complementarily uncharged strands. The conspicuously stable aggregation mechanism observed for FVFLM peptides is found not to conform to the popular 'dock-lock' scheme. We also found high propensity of FVFLM for KLVFF binding. When present, FVFLM disrupts the β-amyloid aggregation pathway and we propose that FVFLM-like peptides might be used to prevent the assembly of full-length Aβ or other pro-amyloidogenic peptides into amyloid fibrils.
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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.