Structure and ordering in localized adsorption of particles

Adamczyk, Zbǐgniew; Zembala, Maria; Siwek, Barbara; Warszyński, Piotr

doi:10.1016/0021-9797(90)90329-m

Cited by 198 publications

(218 citation statements)

References 23 publications

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“…Quantitatively, the structure of particle monolayers can be characterized in terms of the pair correlation function g(r/a) (often referred to as the radial distribution function) (Adamczyk et al 1990Adamczyk 2006;Schaaf and Talbot 1989;Hinrichsen et al 1986). This function expresses the ensemble averaged probability of finding a particle pair at the center to center distance r (normalized usually to particle radius a).…”

Section: Resultsmentioning

confidence: 99%

Irreversible adsorption of latex particles on fibrinogen covered mica

2010

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Physicochemical properties of bovine plasma fibrinogen (Fb) in electrolyte solutions were characterized. These comprised the diffusion coefficient (hydrodynamic radius), determined by the DLS method, electrophoretic mobility and the isoelectric point. The hydrodynamic radius of Fb was 12 nm for pH < 5. The number of uncompensated (electrokinetic) charges on the protein N c was calculated from the electrophoretic mobility data. It was found that for pH < 5.8 the electrokinetic charge was positive, independently of the ionic strength and negative for pH > 5.8. For pH = 3.5 the value of N c , was 26 for 10 −3 M. Similar electrokinetic measurements were performed for the mica substrate using the streaming potential cell. It was shown that for pH = 3.5 and 10 −3 M, the zeta potential of mica remained negative (−50 mV). This promoted an irreversible, electrostatically driven adsorption of Fb, which was confirmed in experiments carried out under diffusion-controlled transport. The surface concentration of Fb on mica was determined directly by AFM counting. By adjusting the time of adsorption, Fb monolayers of desired coverage were produced. Independently, the presence of Fb on mica was determined quantitatively by the colloid enhancement method, in which negatively charged latex particles were used, having the diameter of 800 nm. It was found that for Fb coverage below 0.05 the method was more sensitive than other indirect methods. The experimental data obtained in latex deposition experiments were adequately interpreted in terms of the random site model used previously for polyelectrolytes. It was shown that adsorption sites consisted of a cluster of Z. Adamczyk ( ) · M. Nattich · M. Wasilewska

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Section: Resultsmentioning

confidence: 99%

Irreversible adsorption of latex particles on fibrinogen covered mica

2010

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“…We follow the approach introduced by Adamczyk et al (35,36) to account for the steric effects between bound Abs and define the Ab-Ab interaction energy term, W xh , as…”

Section: Ab-ab Interactionsmentioning

confidence: 99%

Modeling the Role of Epitope Arrangement on Antibody Binding Stoichiometry in Flaviviruses

Ripoll

Khavrutskii

Wallqvist

et al. 2016

Biophysical Journal

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Cryo-electron-microscopy (cryo-EM) structures of flaviviruses reveal significant variation in epitope occupancy across different monoclonal antibodies that have largely been attributed to epitope-level differences in conformation or accessibility that affect antibody binding. The consequences of these variations for macroscopic properties such as antibody binding and neutralization are the results of the law of mass action-a stochastic process of innumerable binding and unbinding events between antibodies and the multiple binding sites on the flavivirus in equilibrium-that cannot be directly imputed from structure alone. We carried out coarse-grained spatial stochastic binding simulations for nine flavivirus antibodies with epitopes defined by cryo-EM or x-ray crystallography to assess the role of epitope spatial arrangement on antibody-binding stoichiometry, occupancy, and neutralization. In our simulations, all epitopes were equally competent for binding, representing the upper limit of binding stoichiometry that results from epitope spatial arrangement alone. Surprisingly, our simulations closely reproduced the relative occupancy and binding stoichiometry observed in cryo-EM, without having to account for differences in epitope accessibility or conformation, suggesting that epitope spatial arrangement alone may be sufficient to explain differences in binding occupancy and stoichiometry between antibodies. Furthermore, we found that there was significant heterogeneity in binding configurations even at saturating antibody concentrations, and that bivalent antibody binding may be more common than previously thought. Finally, we propose a structure-based explanation for the stoichiometric threshold model of neutralization.

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“…III if there is no overlap the virtual particle is added to the existing layer with a probability P (U ) = exp(U/k B T ) [16,17]. Otherwise the virtual dimer is removed and abandoned.…”

Section: Modelmentioning

confidence: 99%

Domain Structure Created by Irreversible Adsorption of Dimers

Barbasz¹,

Cieśla²

2013

Acta Phys. Pol. B

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Structure of monolayers built during adsorption process is strongly related to the properties of adsorbed particles. The most important factor is their shape. For example, adsorption of elongated molecules on patterned surfaces may produce certain orientational order inside a covering layer. This study, however, focuses on random adsorption of dimers on flat, homogeneous surfaces. It has been observed that despite the lack of global orientational ordering, adsorbed dimers may form local, orientationally ordered structures [1,2]. Our investigations focus on the dependence between domain size distribution and environmental parameters such as ionic strength, which affects the range of electrostatic interaction between molecules.

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Structure and ordering in localized adsorption of particles

Cited by 198 publications

References 23 publications

Irreversible adsorption of latex particles on fibrinogen covered mica

Irreversible adsorption of latex particles on fibrinogen covered mica

Modeling the Role of Epitope Arrangement on Antibody Binding Stoichiometry in Flaviviruses

Domain Structure Created by Irreversible Adsorption of Dimers

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