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Red blood cells or erythrocytes, constituting 40 to 45 percent of the total volume of human blood are vesicles filled with hemoglobin with a fluid-like lipid bilayer membrane connected to a 2D spectrin network. The shape, volume, hemoglobin mass, and membrane stiffness of RBCs are important characteristics that influence their ability to circulate through the body and transport oxygen to tissues. In this study, we show that a simple two-LED set up in conjunction with standard microscope imaging can accurately determine the physical and mechanical properties of single RBCs. The Beer–Lambert law and undulatory motion dynamics of the membrane have been used to measure the total volume, hemoglobin mass, membrane tension coefficient, and bending modulus of RBCs. We also show that this method is sensitive enough to distinguish between the mechanical properties of RBCs during morphological changes from a typical discocyte to echinocytes and spherocytes. Measured values of the tension coefficient and bending modulus are 1.27 × 10−6 J m−2 and 7.09 × 10−2 J for discocytes, 4.80 × 10−6 J m−2 and 7.70 × 10−20 J for echinocytes, and 9.85 × 10−6 J m−2 and 9.69 × 10−20 J for spherocytes, respectively. This quantitative light absorption imaging reduces the complexity related to the quantitative imaging of the biophysical and mechanical properties of a single RBC that may lead to enhanced yet simplified point of care devices for analyzing blood cells.

The ongoing COVID-19 pandemic has infected millions of people, claimed hundreds of thousands of lives, and made a worldwide health emergency. Understanding the SARS-CoV-2 mechanism of infection is crucial in the development of potential therapeutics and vaccines. The infection process is triggered by direct binding of the SARS-CoV-2 receptor-binding domain (RBD) to the host cell receptor, Angiotensin-converting enzyme 2 (ACE2). Many efforts have been made to design or repurpose therapeutics to deactivate RBD or ACE2 and prevent the initial binding. In addition to direct inhibition strategies, small chemical compounds might be able to interfere and destabilize the meta-stable, pre-fusion complex of ACE2-RBD. This approach can be employed to prevent the further progress of virus infection at its early stages. In this study, Molecular docking is employed to analyze the binding of two chemical compounds, SSAA09E2 and Nilotinib, with the druggable pocket of the ACE2-RBD complex. The structural changes as a result of the interference with the ACE2-RBD complex are analyzed by molecular dynamics simulations. Results show that both Nilotinib and SSAA09E2 can induce significant conformational changes in the ACE2-RBD complex, intervene with the hydrogen bonds, and influence the flexibility of proteins. Moreover, essential dynamics analysis suggests that the presence of small molecules can trigger large-scale conformational changes that may destabilize the ACE2-RBD complex., Competing Interests: The authors declare no conflict of interest.