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Bromotryptophans and their incorporation in cyclic and bicyclic privileged peptides
Author(s) -
GarcíaPindado Júlia,
Willemse Tom,
Goss Rebecca,
Maes Bert U. W.,
Giralt Ernest,
Ballet Steven,
Teixidó Meritxell
Publication year - 2018
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.23112
Subject(s) - chemistry , bicyclic molecule , cyclic peptide , indole test , tryptophan , residue (chemistry) , amino acid , stereochemistry , amino acid residue , combinatorial chemistry , peptide , biochemistry , peptide sequence , gene
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.