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Frontispiece: Metal‐Free, Site‐Selective Peptide Modification by Conversion of “Customizable” Units into β‐Substituted Dehydroamino Acids
Author(s) -
Saavedra Carlos J.,
Hernández Dácil,
Boto Alicia
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201880364
Subject(s) - peptide , threonine , serine , amino acid , chemistry , hydrolysis , selectivity , combinatorial chemistry , oligopeptide , metal , personalization , stereochemistry , biochemistry , organic chemistry , phosphorylation , catalysis , computer science , world wide web
The site‐selective modification of peptides of serine or threonine units in peptides allowed the generation of β‐substituted dehydro amino acids, which increase peptide resistance to hydrolysis and may improve their biological properties. Both terminal and internal positions can be modified, and different customizable units can be activated separately. Remarkably, high Z selectivity was achieved, even with internal positions. The new dehydroamino acid units were produced under mild and metal‐free conditions. The background of the “Peptide‐Customization Factory” is a view of Tenerife, with the Teide peak towering over the island. More information can be found in the Full Paper by A. Boto et al. on page 599 ff..