Journal
CHEMICAL SOCIETY REVIEWS
Volume 47, Issue 18, Pages 7027-7044Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8cs00278a
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Funding
- American Heart Association: AHA [16SDG31390007]
- Netherlands Organization for Scientific Research [ZonMW Vidi 91713324, ZonMW Vici 91818622]
- NIH [R01 HL118440, R01 HL125703, P01 HL131478, R01 HL144072]
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL118440, R01HL144072, R01HL125703] Funding Source: NIH RePORTER
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Supramolecular systems have applications in areas as diverse as materials science, biochemistry, analytical chemistry, and nanomedicine. However, analyzing such systems can be challenging due to the wide range of time scales, binding strengths, distances, and concentrations at which non-covalent phenomena take place. Due to their versatility and sensitivity, Forster resonance energy transfer (FRET)-based techniques are excellently suited to meet such challenges. Here, we detail the ways in which FRET has been used to study non-covalent interactions in both synthetic and biological supramolecular systems. Among other topics, we examine methods to measure molecular forces, determine protein conformations, monitor assembly kinetics, and visualize in vivo drug release from nanoparticles. Furthermore, we highlight multiplex FRET techniques, discuss the field's limitations, and provide a perspective on new developments.
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