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Ambjörnsson, T.

Publications and source records attributed to Ambjörnsson, T..

3 recordsLinked to original sources

A light-weight segmentation method for multi-state Brownian trajectories

Single-particle tracking methods have emerged as a crucial tool for the characterization of dynamical and diffusive processes in a range of biological and synthetic systems. Here, we propose a simple and light-weight yet accurate method for the segmentation of multi-state Brownian trajectories based on an optimised Gaussian filtering of the displacement time series combined with an automated fitting to a Gaussian mixture model. We verify our method using synthetic, 2-state Brownian trajectories and show that our method provides high levels of accuracy in terms of segmentation and the estimation of self-diffusion coefficients for reasonably well-separated values of the diffusion coefficients. We furthermore demonstrate the feasibility of our method on experimental systems using single-particle tracking data for diffusing membrane proteins bound to a supported lipid bilayer. Compared to methods based on deep learning or hidden Markov models our method imposes a much lower computational load, making it suitable for fast and accurate online processing of single-particle trajectories from microscopy images.

biophysics↗

Random sampling of ligand arrangements on a one-dimensional lattice

We introduce a transfer-matrix-based sequential sampling scheme for generating random samples of ligand arrangements on one-dimensional templates. The number of ligand types is arbitrary, the binding constants can have positional dependence, and cooperativity parameters are included. From the random arrangements, any (linear or non-linear) observable can be calculated using sample averaging. We provide a publically available software with a computational time that scales linearly with the lattice size. As an example application, we study the competitive binding of three ligand types (the sequence-specific binder netropsin, YOYO-1 and ethidium bromide) to a DNA molecule.

biophysics↗

A predictive model of antibody binding in the presence of IgG-interacting bacterial surface proteins

Many bacteria can interfere with how antibodies bind to their surfaces. This bacterial antibody targeting makes it challenging to predict the immunological function of bacteria-associated antibodies. The M and M-like proteins of group A streptococci exhibit IgGFc-binding regions, which they use to reverse IgG binding orientation depending on the host environment. Unraveling the mechanism behind these binding characteristics may identify conditions under which bound IgG can drive an efficient immune response. Here, we have developed a biophysical model for describing these complex protein-antibody interactions. We show how the model can be used as a tool for studying various IgG samples behaviour by performing in silico simulations and correlating this data with experimental measurements. Besides its use for mechanistic understanding, this model could potentially be used as a tool to predict the effect, as well as aid in the development of antibody treatments. We illustrate this by simulating how IgG binding in serum is altered as specified amounts of monoclonal or pooled IgG is added. Phagocytosis experiments link this altered antibody binding to a physiological function and demonstrate that it is possible to predict the effect of an IgG treatment with our model. Our study gives a mechanistic understanding of bacterial antibody targeting and provides a tool for predicting the effect of antibody treatments.

microbiology↗