RT Journal Article
T1 C60-based Multivalent Glycoporphyrins Inhibit SARS-CoV-2 Specific Interaction with the DC-SIGN Transmembrane Receptor
A1 Patino Alonso, Jennifer
A1 Cabrera González, Justo Enrique
A1 Merino Gracia, Javier
A1 Nieta-Ortiz, Gema
A1 Katati, Jouma
A1 Bezerra da Cruz, Carlos
A1 Mateos Gil, Pablo
A1 Canales Mayordomo, María Ángeles
A1 López Montero, Iván
A1 Illescas Martínez, Beatriz María
A1 Delgado Vázquez, Rafael
A1 Martín León, Nazario
AB 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.
PB Wiley
SN 1613-6810
YR 2023
FD 2023
LK https://hdl.handle.net/20.500.14352/98371
UL https://hdl.handle.net/20.500.14352/98371
LA eng
NO 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.
NO Ministerio de Ciencia, Innovación y Universidades (España)
NO European Commission
DS Docta Complutense
RD 31 ago 2024