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Updated: Jul 27, 2026

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer
Published on: August 20, 2012
@-tides as reporters for molecular associations
Scott T Phillips1, Landy K Blasdel, Paul A Bartlett
1Center for New Directions in Organic Synthesis, Department of Chemistry, University of California, Berkeley, California 94720-1460, USA.
Abstract:
The 1,6-dihydro-3(2H)-pyridinone unit is an amino acid surrogate that favors the extended beta-strand conformation when incorporated in an oligopeptide ("@-tide") strand. We now report that the circular dichroism (CD) signature of the vinylogous amide in the @-unit is sensitive to conformation in organic and aqueous solvents and, therefore, is useful as a quantitative measure of @-tide association and folding processes that involve this moiety. Moreover, this method can be employed in the micromolar concentration range, which is not readily accessible using other techniques. Measurements of @-tide dimerization and beta-hairpin folding equilibria not only demonstrate the utility and generality of this approach but also provide a way to quantify amino acid side chain-side chain interactions relevant to beta-sheet stability.
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