ArticleThe Journal of biological chemistry2014
Computational and experimental studies on β-sheet breakers targeting Aβ1-40 fibrils.
Article in The Journal of biological chemistry, 2014. 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, 79 citations in OpenAlex.
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- A Snake Venom Peptide and Its Derivatives Prevent AβACS chemical neuroscience · 2024Article
- Delineating the Role of GxxxG Motif in Amyloidogenesis: A New Perspective in Targeting Amyloid-Beta Mediated AD Pathogenesis.ACS bio & med chem Au · 2024Review
- AβACS chemical neuroscience · 2023Article
- Influence of Cortisol on the Fibril Formation Kinetics of Aβ42 Peptide: A Multi-Technical Approach.International journal of molecular sciences · 2022Article
- Effect of Date Palm (Frontiers in neuroscience · 2022Article
- Destabilization potential of beta sheet breaker peptides on Abeta fibril structure: an insight from molecular dynamics simulation study.RSC advances · 2021Article
- Amyloid-β-Derived Peptidomimetics Inhibits Tau Aggregation.ACS omega · 2021Article
- Peptide-Protein Interactions: From Drug Design to Supramolecular Biomaterials.Molecules (Basel, Switzerland) · 2021Review
- Invasive and non-invasive therapies for Alzheimer's disease and other amyloidosis.Biophysical reviews · 2020Review
- Multivalent Polymer-Peptide Conjugates-A General Platform for Inhibiting Amyloid Beta Peptide Aggregation.ACS macro letters · 2019Article
- Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms.International journal of molecular sciences · 2018Review
- Oligomerization Alters Binding Affinity Between Amyloid Beta and a Modulator of Peptide Aggregation.The journal of physical chemistry. C, Nanomaterials and interfaces · 2017Article
- Single-Nucleotide Polymorphism of PPARγ, a Protein at the Crossroads of Physiological and Pathological Processes.International journal of molecular sciences · 2017Article
- Chitosan Oligosaccharides Inhibit/Disaggregate Fibrils and Attenuate Amyloid β-Mediated Neurotoxicity.International journal of molecular sciences · 2015Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this work we present and compare the results of extensive molecular dynamics simulations of model systems comprising an Aβ1-40 peptide in water in interaction with short peptides (β-sheet breakers) mimicking the 17-21 region of the Aβ1-40 sequence. Various systems differing in the customized β-sheet breaker structure have been studied. Specifically we have considered three kinds of β-sheet breakers, namely Ac-LPFFD-NH2 and two variants thereof, one obtained by substituting the acetyl group with the sulfonic amino acid taurine (Tau-LPFFD-NH2) and a second novel one in which the aspartic acid is substituted by an asparagine (Ac-LPFFN-NH2). Thioflavin T fluorescence, circular dichroism, and mass spectrometry experiments have been performed indicating that β-sheet breakers are able to inhibit in vitro fibril formation and prevent the β sheet folding of portions of the Aβ1-40 peptide. We show that molecular dynamics simulations and far UV circular dichroism provide consistent evidence that the new Ac-LPFFN-NH2 β-sheet breaker is more effective than the other two in stabilizing the native α-helix structure of Aβ1-40. In agreement with these results thioflavin T fluorescence experiments confirm the higher efficiency in inhibiting Aβ1-40 aggregation. Furthermore, mass spectrometry data and molecular dynamics simulations consistently identified the 17-21 Aβ1-40 portion as the location of the interaction region between peptide and the Ac-LPFFN-NH2 β-sheet breaker.
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