ArticleJournal of chemical theory and computation2020
d-Retro Inverso Amylin and the Stability of Amylin Fibrils.
Article in Journal of chemical theory and computation, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Modulation of AβJournal of chemical information and modeling · 2025Article
- Genome Editing in Ferret Airway Epithelia Mediated by CRISPR/Nucleases Delivered with Amphiphilic Shuttle Peptides.Human gene therapy · 2023Article
- Human Amylin in the Presence of SARS-COV-2 Protein Fragments.ACS omega · 2023Article
- Effect of an Amyloidogenic SARS-COV-2 Protein Fragment on α-Synuclein Monomers and Fibrils.The journal of physical chemistry. B · 2022Article
- Small Peptides for Inhibiting Serum Amyloid A Aggregation.ACS medicinal chemistry letters · 2021Article
- Recent Applications of Retro-Inverso Peptides.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Motivated by the role that amylin aggregates play in type-II diabetes, we compare the stability of regular amylin fibrils with the stability of fibrils where l-amino acid chains are replaced by d-retro inverso (DRI) amylin, that is, peptides where the sequence of amino acids is reversed, and at the same time, the l-amino acids are replaced by their mirror images. Our molecular dynamics simulations show that despite leading to only a marginal difference in the fibril structure and stability, aggregating DRI-amylin peptides have different patterns of contacts and hydrogen bonding. Because of these differences, DRI-amylin, when interacting with regular (l) amylin, alters the elongation process and lowers the stability of hybrid amylin fibrils. Our results not only suggest the potential use of DRI-amylin as an inhibitor of amylin fibril formation but also point to the possibility of using the insertion of DRI proteins in l-assemblies as a way to probe the role of certain kinds of hydrogen bonds in supramolecular assemblies or aggregates.
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Registered trials
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