2026-04-13T00:51:55Zhttps://recercat.cat/oai/request
oai:recercat.cat:2445/1210622025-12-04T19:32:47Zcom_2072_1057col_2072_478908col_2072_478917col_2072_478933
RECERCAT author García Pindado, Júlia author Willemse, Tom author Goss, Rebecca author Maes, Bert U. W. author Giralt Lledó, Ernest author Ballet, Steven author Teixidó Turà, Meritxell 2018-03-23T11:32:07Z2019-03-12T06:10:23Z2018-03-122018-03-22T08:17:37Z While revisiting biologically active natural peptides, the importance of the tryptophan residue became clear. In this article, the incorporation of this amino acid, brominated at different positions of the indole ring, into cyclic peptides was successfully achieved. These products demonstrated improved properties in terms of passive diffusion, permeability across membranes, biostability in human serum and cytotoxicity. Moreover, these brominated tryptophans at positions 5, 6, or 7 proved to be compatible as building blocks to prepare bicyclic stapled peptides by performing on‐resin Suzuki‐Miyaura cross‐coupling reactions. (c) Wiley, 2018 info:eu-repo/semantics/openAccess Pèptids Triptòfan Peptides Tryptophan Bromotryptophans and their incorporation in cyclic and bicyclic privileged peptides info:eu-repo/semantics/article info:eu-repo/semantics/acceptedVersion