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A 3D Peptide/[60]Fullerene Hybrid for Multivalent Recognition

Fully substituted peptide/[60]fullerene hexakis‐adducts offer an excellent opportunity for multivalent protein recognition. In contrast to monofunctionalized fullerene hybrids, peptide/[60]fullerene hexakis‐adducts display multiple copies of a peptide in close spatial proximity and in the three dime...

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Detalles Bibliográficos
Autores principales: Gallego, Iván, Ramos‐Soriano, Javier, Méndez‐Ardoy, Alejandro, Cabrera‐González, Justo, Lostalé‐Seijo, Irene, Illescas, Beatriz M., Reina, Jose J., Martín, Nazario, Montenegro, Javier
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9826239/
https://www.ncbi.nlm.nih.gov/pubmed/35989251
http://dx.doi.org/10.1002/anie.202210043
Descripción
Sumario:Fully substituted peptide/[60]fullerene hexakis‐adducts offer an excellent opportunity for multivalent protein recognition. In contrast to monofunctionalized fullerene hybrids, peptide/[60]fullerene hexakis‐adducts display multiple copies of a peptide in close spatial proximity and in the three dimensions of space. High affinity peptide binders for almost any target can be currently identified by in vitro evolution techniques, often providing synthetically simpler alternatives to natural ligands. However, despite the potential of peptide/[60]fullerene hexakis‐adducts, these promising conjugates have not been reported to date. Here we present a synthetic strategy for the construction of 3D multivalent hybrids that are able to bind with high affinity the E‐selectin. The here synthesized fully substituted peptide/[60]fullerene hybrids and their multivalent recognition of natural receptors constitute a proof of principle for their future application as functional biocompatible materials.