ArticleThe Journal of chemical physics2013
Dual effect of crowders on fibrillation kinetics of polypeptide chains revealed by lattice models.
Article in The Journal of chemical physics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 25 citations in OpenAlex.
- Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation.Molecules (Basel, Switzerland) · 2022Review
- Computational Models for the Study of Protein Aggregation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Effect of Surface Roughness on Aggregation of Polypeptide Chains: A Monte Carlo Study.Biomolecules · 2021Article
- Kinetics and mechanical stability of the fibril state control fibril formation time of polypeptide chains: A computational study.The Journal of chemical physics · 2018Article
- Physical mechanism for biopolymers to aggregate and maintain in non-equilibrium states.Scientific reports · 2017Article
- Effects of hydrophobic macromolecular crowders on amyloid β (16-22) aggregation.Biophysical journal · 2015Article
- Effects of macromolecular crowding on amyloid beta (16-22) aggregation using coarse-grained simulations.The journal of physical chemistry. B · 2014Article
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Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have developed the lattice model for describing polypeptide chains in the presence of crowders. The influence of crowding confinement on the fibrillation kinetics of polypeptide chains is studied using this model. We observed the non-trivial behavior of the fibril formation time τfib that it decreases with the concentration of crowders if crowder sizes are large enough, but the growth is observed for crowders of small sizes. This allows us to explain the recent experimental observation on the dual effect of crowding particles on fibril growth of proteins that for a fixed crowder concentration the fibrillation kinetics is fastest at intermediate values of total surface of crowders. It becomes slow at either small or large coverages of cosolutes. It is shown that due to competition between the energetics and entropic effects, the dependence of τfib on the size of confined space is described by a parabolic function.
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