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Self-Assembly of Microscopic Rods Due to Depletion Interaction.

ABSTRACT: In this article, using numerical simulations we investigate the self-assembly of rod-like particles in suspension due to depletion forces which naturally emerge due to the presence of smaller spherical depletant particles. We characterize the type of clusters that are formed and the evolution of aggregation departing from a random initial configuration. We show that eventually the system reaches a thermodynamic equilibrium state in which the aggregates break and reform dynamically. We investigate the equilibrium state of aggregation, which exhibits a strong dependence on depletant concentration. In addition, we provide a simple thermodynamic model inspired on the theory of self-assembly of amphiphilic molecules which allows us to understand qualitatively the equilibrium aggregate size distributions that we obtain in simulation.

SUBMITTER: Calero C

PROVIDER: S-EPMC7597238 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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Self-Assembly of Microscopic Rods Due to Depletion Interaction.

Calero Carles C Pagonabarraga Ignacio I

Entropy (Basel, Switzerland) 20201001 10

In this article, using numerical simulations we investigate the self-assembly of rod-like particles in suspension due to depletion forces which naturally emerge due to the presence of smaller spherical depletant particles. We characterize the type of clusters that are formed and the evolution of aggregation departing from a random initial configuration. We show that eventually the system reaches a thermodynamic equilibrium state in which the aggregates break and reform dynamically. We investigat ...[more]

PMID: 33286883

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Project description:Amelogenin and ameloblastin are 2 extracellular matrix proteins that are essential for the proper development of enamel. We recently reported that amelogenin and ameloblastin colocalized during the secretory stage of enamel formation when nucleation of enamel crystallites occurs. Direct interactions between the 2 proteins have been also demonstrated in our in vitro studies. Here, we explore interactions between their fragments during enamel maturation. We applied in vivo immunofluorescence imaging, quantitative co-localization analysis, and a new FRET (fluorescence resonance energy transfer) technique to demonstrate ameloblastin and amelogenin interaction in the maturing mouse enamel. Using immunochemical analysis of protein samples extracted from 8-d-old (P8) first molars from mice as a model for maturation-stage enamel, we identified the ~17-kDa ameloblastin (Ambn-N) and the TRAP (tyrosine-rich amelogenin peptide) fragments. We used Ambn-N18 and Ambn-M300 antibodies raised against the N-terminal and C-terminal segments of ameloblastin, as well as Amel-FL and Amel-C19 antibodies against full-length recombinant mouse amelogenin (rM179) and C-terminal amelogenin, respectively. In transverse sections, co-localization images of N-terminal fragments of amelogenin and ameloblastin around the prism boundary revealed the "fish net" pattern of the enamel matrix. Using in vivo FRET microscopy, we further demonstrated spatial interactions between amelogenin and ameloblastin N-terminal fragments. In the maturing mouse enamel, the association of these residual protein fragments created a discontinuity between enamel rods, which we suggest is important for support and maintenance of enamel rods and eventual contribution to unique enamel mechanical properties. We present data that support cooperative functions of enamel matrix proteins in mediating the structural hierarchy of enamel and that contribute to our efforts to design and develop enamel biomimetic material.

Dataset Information

Self-Assembly of Microscopic Rods Due to Depletion Interaction.

Publications

Self-Assembly of Microscopic Rods Due to Depletion Interaction.

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