Premium
4‐Aminophthalimide Amino Acids as Small and Environment‐Sensitive Fluorescent Probes for Transmembrane Peptides
Author(s) -
Wörner Samantha,
Rönicke Franziska,
Ulrich Anne S.,
Wagenknecht HansAchim
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900520
Subject(s) - fluorescence , chemistry , indole test , tryptophan , amino acid , moiety , transmembrane protein , liposome , fluorescence in the life sciences , chromophore , circular dichroism , lipid bilayer , aromatic amino acids , fluorescence spectroscopy , biophysics , membrane , photochemistry , stereochemistry , biochemistry , biology , physics , receptor , quantum mechanics
Fluorescence probing of transmembrane (TM) peptides is needed to complement state‐of‐the art methods—mainly oriented circular dichroism and solid‐state NMR spectroscopy—and to allow imaging in living cells. Three new amino acids incorporating the solvatofluorescent 4‐aminophthalimide in their side chains were synthesized in order to examine the local polarity in the α‐helical TM fragment of the human epidermal growth factor receptor. It was possible to distinguish their locations, either in the hydrophobic core of the lipid bilayer or at the membrane surface, by fluorescence readout, including blue shift and increased quantum yield. An important feature is the small size of the 4‐aminophthalimide chromophore. It makes one of the new amino acids approximately isosteric to tryptophan, typically used as a very small fluorescent amino acid in peptides and proteins. In contrast to the only weakly fluorescent indole system in tryptophan, the 4‐aminophthalimide moiety produces a significantly more informative fluorescence readout and is selectively excited outside the biopolymer absorption range.