Tag Archive for: liposomes

Publication on AWSensors technology

C60-based Multivalent Glycoporphyrins Inhibit SARS-CoV-2 Specific Interaction with the DC-SIGN Transmembrane Receptor

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Authors: Jennifer Patino-Alonso, Justo Cabrera-González, Javier Merino, Gema Nieto-Ortiz, Fátima Lasala, Jouma Katati, Carlos H. Bezerra da Cruz, Ajay K. Monnappa, Pablo Mateos-Gil, Ángeles Canales, Iván López-Montero, Beatriz M. Illescas, Rafael Delgado, and Nazario Martín

Journal: Small (2023)

 

Abstract

Since WHO has declared the COVID-19 outbreak a global pandemic, nearly seven million deaths have been reported. This efficient spread of Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2) is facilitated by the ability of the spike glycoprotein to bind multiple cell membrane receptors. Although ACE2 is identified as the main receptor for SARS-CoV-2, other receptors could play a role in viral entry. Among others, C-type lectins such as DC-SIGN are identified as efficient trans-receptor for SARS-CoV-2 infection, so the use of glycomimetics to inhibit the infection through the DC-SIGN blockade is an encouraging approach. In this regard, multivalent nanostructures based on glycosylated [60]fullerenes linked to a central porphyrin scaffold have been designed and tested against DC-SIGN-mediated SARS-CoV-2 infection. First results show an outstanding inhibition of the trans-infection up to 90%. In addition, a deeper understanding of nanostructure-receptor binding is achieved through microscopy techniques, high-resolution NMR experiments, Quartz Crystal Microbalance experiments, and molecular dynamic simulations.

You may read the full paper here.

Publication on AWSensors technology

Membrane insertion mechanism of the caveola coat protein Cavin1

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Authors: Liu, K.-C., Pace, H., Larsson, E., Hossain, S., Kabedev, A., Shukla, A., Jerschabek, V., Mohan, J., Bergström, C. A. S., Bally, M., Schwieger, C., Hubert, M., & Lundmark, R.

Journal: PNAS (2022)

 

Abstract

Caveolae are small plasma membrane invaginations, important for control of membrane tension, signaling cascades, and lipid sorting. The caveola coat protein Cavin1 is essential for shaping such high curvature membrane structures. Yet, a mechanistic understanding of how Cavin1 assembles at the membrane interface is lacking. Here, we used model membranes combined with biophysical dissection and computational modeling to show that Cavin1 inserts into membranes. We establish that initial phosphatidylinositol (4, 5) bisphosphate [PI(4,5)P2]–dependent membrane adsorption of the trimeric helical region 1 (HR1) of Cavin1 mediates the subsequent partial separation and membrane insertion of the individual helices. Insertion kinetics of HR1 is further enhanced by the presence of flanking negatively charged disordered regions, which was found important for the coassembly of Cavin1 with Caveolin1 in living cells. We propose that this intricate mechanism potentiates membrane curvature generation and facilitates dynamic rounds of assembly and disassembly of Cavin1 at the membrane.

You may read the full paper here.