Separating and analyzing DNA, RNA or proteins is often done through gel electrophoresis. This simple technique is conducted millions of times in labs every day world-wide. Analysis of the gels is typically done visually on a photo by comparing measured intensities with a well-defined reference ladder. Using digital photography and image analysis, we have developed a technique to quantitatively analyze standard gel images to determine exact sized distributions. This information can then be used to compare experimental data to theoretical models and predictions. The software consists of a smartphone-based application with an easy-to-use GUI to analyze images of any quality, dimension, or type. Within seconds, the user can sign in, choose ladder specifications, and select the image for analysis. They can then tap on the ladders of interest and send the image for analysis. The cloud-based analysis uses an exponential model to characterize the propagation of molecules within the gel and automatically measures the size and relative quantity of detectable solutes. I will provide direct evidence that the software allows measurement of RNA molecule lengths with resolution down to a single monomer. The entire analysis process takes under 10 seconds, after which the results are automatically emailed to the user. The novel way in which this data is processed and presented to the end-user in a seamlessly integrated workflow with possibilities for additional integration makes this a major step forward over existing solutions. Enabling, supporting, and promoting this research by creating easy-to-use and powerful tools has the potential to promote change in physical and biological research.

The quantitative analysis of gel electrophoresis data using a cloud-based smartphone application

More than 30 million individuals worldwide are living with Alzheimer’s Disease. To further the current understanding on this neurodegenerative disease, we developed a technique to create amyloid peptide clusters in synthetic, brain-like membranes, which mimic the senile plaques found in the brains of Alzheimer's patients. I compared the molecular functioning of homotaurine, a peptic anti-aggregant that binds to amyloid peptides directly, and curcumin, a non-peptic molecule that can inhibit aggregation by changing membrane properties. By using microscopy, x-ray diffraction, and UV-vis spectroscopy, we found that both curcumin and homotaurine significantly reduce the number of small, nanoscopic amyloid aggregates and the corresponding β- and cross-β sheet signals. This research shows that membrane active drugs can be as efficient as peptide targeting drugs in inhibiting amyloid aggregation in-vitro [1]. The findings can open new pathways for the developments of drugs to slow down first occurrence and progression of the disease.

[1] Xingyuan Zou, Sebastian Himbert, Janos Juhasz, Samantha Ros, Harald D. H. Stover, and Maikel C. Rheinstädter, “Curcumin and homotaurine suppress amyloid-b25-35 aggregation in synthetic brain membranes”, under review with ACS Chemical Neuroscience, Manuscript ID: cn-2021-00057r

Curcumin and homotaurine suppress amyloid-b25-35 aggregation in synthetic brain membranes

Blood banks all around the world store blood for several weeks ensuring the availability of blood for transfusion medicine. Although the storage conditions have been optimized for decades it has become evident that red blood cells (RBC) undergo numerous changes when being stored.
We investigated the effect of storage on the nanoscopic bending rigidity of RBC membranes with a combination of Molecular Dynamics simulations, inelastic neutron scattering and diffuse X-ray scattering [1]. Coarse grained (CG) models of RBC membranes were created by matching experimental lipidomic analysis. It was found experimentally that the concentration of fatty acids and cholesterol changes during storage and aged membranes were mimicked by adjusting the lipid composition accordingly. 
Solid supported membrane stacks of fresh and stored RBC samples were prepared. X-ray diffraction experiments were then conducted at high relative humidity allowing to reconstruct the membrane surface fluctuations from diffuse scattering signals using a GPU accelerated workstation. These experiments were complemented by Neutron Spin Echo measurements on RBC vesicles which probe the membrane fluctuations directly. Bending moduli of 1.8 kBT and 15.4 kBT were measured in excellent agreement with the simulation data.
[1] Himbert et al., “The Nanoscopic Bending Rigidity of Red Blood Cell Membranes”, in preparation

THE NANOSCOPIC BENDING RIGIDITY OF RED BLOOD CELL MEMBRANES

<i>**Session Chair: ** Melanie Campbell</i>

W3-4 Molecular and Cellular Biophysics (DPMB) / Biophysique moléculaire et biophysique cellulaire (DPMB)

technical paper

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Sebastian Himbert

6

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The quantitative analysis of gel electrophoresis data using a cloud-based smartphone application

Curcumin and homotaurine suppress amyloid-b25-35 aggregation in synthetic brain membranes

THE NANOSCOPIC BENDING RIGIDITY OF RED BLOOD CELL MEMBRANES

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