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oai:docta.ucm.es:20.500.14352/983712025-03-18T15:53:07Zcom_20.500.14352_14col_20.500.14352_15

C60-based Multivalent Glycoporphyrins Inhibit SARS-CoV-2 Specific Interaction with the DC-SIGN Transmembrane Receptor Patino Alonso, Jennifer Cabrera González, Justo Enrique Merino Gracia, Javier Nieta Ortiz, Gema Katati, Jouma Bezerra Da Cruz, Carlos Mateos Gil, Pablo Canales Mayordomo, María Ángeles López Montero, Iván Illescas Martínez, Beatriz María Delgado Vázquez, Rafael Martín León, Nazario 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. 2024-02-02T14:52:07Z 2024-02-02T14:52:07Z 2023 journal article Patino‐Alonso, Jennifer, et al. «C 60 ‐based Multivalent Glycoporphyrins Inhibit SARS‐CoV‐2 Specific Interaction with the DC‐SIGN Transmembrane Receptor». Small, vol. 20, n.o 19, mayo de 2024, p. 2307045. https://doi.org/10.1002/smll.202307045. 1613-6810 10.1002/smll.202307045 https://hdl.handle.net/20.500.14352/98371 https://doi.org/10.1002/smll.202307045 eng open access Wiley