2026-08-29T14:07:38Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/188092024-09-21T21:00:49Zcom_20.500.12105_15322com_20.500.12105_2051col_20.500.12105_16927

00925njm 22002777a 4500 dc Gallego, Iván author Ramos-Soriano, Javier author Méndez-Ardoy, Alejandro author Cabrera-González, Justo author Lostalé-Seijo, Irene author Illescas, Beatriz M author Reina, Jose J author Martín, Nazario author Montenegro, Javier author 2022-09-06 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. 10.1002/anie.202210043 1521-3773 Angewandte Chemie (International ed. in English) http://hdl.handle.net/10668/20396 35989251 http://hdl.handle.net/20.500.12105/18809 Fullerenes Glycomimetic Lectin Multivalency Peptides A 3D Peptide/[60]Fullerene Hybrid for Multivalent Recognition.