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A Polarity‐Sensitive Fluorescent Amino Acid and its Incorporation into Peptides for the Ratiometric Detection of Biomolecular Interactions
Author(s) -
Yokoo Hidetomo,
Kagechika Hiroyuki,
Ohsaki Ayumi,
Hirano Tomoya
Publication year - 2019
Publication title -
chempluschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.801
H-Index - 61
ISSN - 2192-6506
DOI - 10.1002/cplu.201900489
Subject(s) - fluorescence , fluorophore , calmodulin , peptide , chemistry , polarity (international relations) , amino acid , aqueous solution , solvent polarity , solvent , combinatorial chemistry , biophysics , biochemistry , organic chemistry , enzyme , biology , physics , quantum mechanics , cell
Abstract A fluorescent amino acid containing our recently developed 1,5‐naphthyridin‐2(1 H )‐one based‐ fluorophore, which is a structural component of the fluorescent natural compounds amarastelline A and nigakinone, has been developed. It has useful functions, that is, solvent‐polarity‐dependent change of fluorescence ratio at 370/480 nm and strong fluorescence in both aqueous solution and less polar organic solvents. To demonstrate its utility, it was incorporated into a C5 peptide with the aim of detecting the interaction of this peptide with calmodulin. As expected, the fluorescence ratio at 370/480 nm of the peptide was changed by the calmodulin only in the presence of Ca 2+ , thus indicating that the fluorescent peptide could sense the conformational change of calmodulin induced by Ca 2+ , followed by its interaction. These results also suggest that this fluorescent amino acid as well as its precursor, a succinimidyl ester, could be applicable for detecting various biomolecular interactions.