ArticleEuropean biophysics journal : EBJ2015
Mechanisms of the self-assembly of EAK16-family peptides into fibrillar and globular structures: molecular dynamics simulations from nano- to micro-seconds.
Article in European biophysics journal : EBJ, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 19 citations in OpenAlex.
- A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides.Gels (Basel, Switzerland) · 2023Article
- Active tyrosine phenol-lyase aggregates induced by terminally attached functional peptides in Escherichia coli.Journal of industrial microbiology & biotechnology · 2020Article
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5 authors at 1 institution in 1 country.
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Abstract
The self-assembly of EAK16-family peptides in a bulk solution was studied using a combination of all-atom and coarse-grained molecular dynamics simulations. In addition, specified concentrations of EAK16 peptides were induced to form fibrillary or globular assemblies in vitro. The results show that the combination of all-atom molecular dynamics simulations on the single- and double-chain levels and coarse-grained simulations on the many-chain level predicts the experimental observations reasonably well. At neutral pH conditions, EAK16-I and EAK16-II assemble into fibrillary structures, whereas EAK16-IV aggregates into globular assemblies. Mechanisms of the formation of fibrillar and globular assemblies are described using the simulation results.
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